Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90348-5
I Ohkubo, C Namikawa, S Higashiyama, M Sasaki, O Minowa, Y Mizuno, H Shiokawa
1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.
{"title":"Purification and characterization of alpha 1-thiol proteinase inhibitor and its identity with kinin- and fragment 1.2-free high molecular weight kininogen.","authors":"I Ohkubo, C Namikawa, S Higashiyama, M Sasaki, O Minowa, Y Mizuno, H Shiokawa","doi":"10.1016/0020-711x(88)90348-5","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90348-5","url":null,"abstract":"<p><p>1. alpha 1-Thiol proteinase inhibitor (alpha 1 TPI) purified from outdated human plasma was a glycoprotein with Mr 83,000 and was composed of heavy and light chains held together with a disulfide bond. 2. The data on amino acid composition, amino terminal sequence of the light chain and carboxyl terminal sequences of the heavy and light chains indicate that alpha 1 TPI is identical with kinin- and fragment 1.2-free HMW kininogen. 3. Purified human plasmin generated a derivative having the same molecular weight (Mr 83,000), same subunit structure (heavy and light chains) and same inhibitory capacity as alpha 1 TPI from HMW kininogen and kinin-free HMW kininogen. This indicated the possibility that alpha 1 TPI is derived from HMW kininogen by plasmin.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90348-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14482758","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90350-3
C Challen, D H Adams
1. Conventional DNA extraction procedures have failed to release free DNA from the chick embryo fibroblast cytosolic DNA-RNA complexes. 2. Free DNA has been released only from the smallest cell cytosol DNA fraction, which is not in the native state associated with RNA: it is very small (of the order of 100 bases) and single stranded. 3. However, phenol extraction does separate complex DNA-associated material from the RNA which has invariably been found to accompany it in all but the smallest fraction (see 2 above). 4. The principal factor preventing DNA release appears to be a massive aggregation of partially purified DNA-associated material.
{"title":"The search for the DNA of the chick embryo fibroblast cytosolic complex.","authors":"C Challen, D H Adams","doi":"10.1016/0020-711x(88)90350-3","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90350-3","url":null,"abstract":"<p><p>1. Conventional DNA extraction procedures have failed to release free DNA from the chick embryo fibroblast cytosolic DNA-RNA complexes. 2. Free DNA has been released only from the smallest cell cytosol DNA fraction, which is not in the native state associated with RNA: it is very small (of the order of 100 bases) and single stranded. 3. However, phenol extraction does separate complex DNA-associated material from the RNA which has invariably been found to accompany it in all but the smallest fraction (see 2 above). 4. The principal factor preventing DNA release appears to be a massive aggregation of partially purified DNA-associated material.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90350-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13597311","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90355-2
M T Hincke
1. Protein kinase C (PK-C) from the rat parotid gland has been partially purified and characterized for the first time. During its purification, this enzyme exhibited the same chromatographic behavior as the rat brain enzyme. 2. Affinities for phosphatidylserine (3 micrograms/ml), ATP (8 microM) and calcium (8 microM) were determined kinetically and found to be similar for the enzymes from each tissue. 3. Experiments designed to detect agonist-stimulated translocation of PK-C activity during phosphatidylinositol turnover found no change in levels of soluble PK-C, suggesting that PK-C translocation may not be an obligatory correlate of its activation. The implications of this result are discussed.
{"title":"Characterization of rat parotid protein kinase C.","authors":"M T Hincke","doi":"10.1016/0020-711x(88)90355-2","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90355-2","url":null,"abstract":"<p><p>1. Protein kinase C (PK-C) from the rat parotid gland has been partially purified and characterized for the first time. During its purification, this enzyme exhibited the same chromatographic behavior as the rat brain enzyme. 2. Affinities for phosphatidylserine (3 micrograms/ml), ATP (8 microM) and calcium (8 microM) were determined kinetically and found to be similar for the enzymes from each tissue. 3. Experiments designed to detect agonist-stimulated translocation of PK-C activity during phosphatidylinositol turnover found no change in levels of soluble PK-C, suggesting that PK-C translocation may not be an obligatory correlate of its activation. The implications of this result are discussed.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90355-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481970","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90358-8
W Dobryszycka, T Guszczyński
1. Tyrosine and two structural isomers of histidine residues in human haptoglobin were modified with diazotized sulfanilic acid. Sulfanilazo-derivatives of haptoglobin obtained by increasing the reagent/protein molar ration showed gradual decrease of peroxidase activity when complexed with hemoglobin. 2. Formation of haptoglobin derivatives with ten mono(sulfanilazo)-tyrosines and two mono (sulfanilazo)histidines resulted in the blockage of one out of six antigenic determinants, whereas immunoreactivity of the derivative with fourteen azotyrosines, one C-4, and two C-2 azohistidines was decreased by half. 3. Removal of sialic acid from oligosaccharide chains of haptoglobin made the molecule more accessible to diazotized sulfanilic acid. 4. Sulfanilazo-modification of tyrosine and histidine residues was practically of no effect in the reaction of haptoglobin with plant lectin, concanavalin A.
{"title":"Properties of sulfanilazo-haptoglobin.","authors":"W Dobryszycka, T Guszczyński","doi":"10.1016/0020-711x(88)90358-8","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90358-8","url":null,"abstract":"<p><p>1. Tyrosine and two structural isomers of histidine residues in human haptoglobin were modified with diazotized sulfanilic acid. Sulfanilazo-derivatives of haptoglobin obtained by increasing the reagent/protein molar ration showed gradual decrease of peroxidase activity when complexed with hemoglobin. 2. Formation of haptoglobin derivatives with ten mono(sulfanilazo)-tyrosines and two mono (sulfanilazo)histidines resulted in the blockage of one out of six antigenic determinants, whereas immunoreactivity of the derivative with fourteen azotyrosines, one C-4, and two C-2 azohistidines was decreased by half. 3. Removal of sialic acid from oligosaccharide chains of haptoglobin made the molecule more accessible to diazotized sulfanilic acid. 4. Sulfanilazo-modification of tyrosine and histidine residues was practically of no effect in the reaction of haptoglobin with plant lectin, concanavalin A.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90358-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481974","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90360-6
B P Dias Filho, C S Alviano, W de Souza, J Angluster
1. The polysaccharide and glycolipid composition in Tritrichomonas foetus was studied by paper, thin-layer and gas-liquid chromatographic analysis. 2. The carbohydrate components of the polysaccharide were glucose (47%), galactose (34%) and mannose (19%). N-acetylneuraminic acid was the sialic acid derivative characterized in the flagellate whole cells. 3. The sialic acid density was estimated as 2.7 x 10(7) residues/cell. 4. The long-chain base dihydrosphingosine, the carbohydrates galactose (67%), glucose (21%) and mannose (12%) as well as the fatty acids myristic (48%) and palmitic (52%) acids were characterized as components of the total glycolipids of T. foetus. 5. Total glycolipids were fractionated: a galactocerebroside and a ganglioside were identified.
1. 采用纸层色谱、薄层色谱和气液色谱等分析方法对毛滴虫胎儿的多糖和糖脂组成进行了研究。2. 多糖的碳水化合物成分为葡萄糖(47%)、半乳糖(34%)和甘露糖(19%)。n -乙酰神经氨酸是鞭毛虫全细胞中所特有的唾液酸衍生物。3.唾液酸密度估计为2.7 x 10(7)个残基/细胞。4. 长链碱基二氢鞘氨醇、碳水化合物半乳糖(67%)、葡萄糖(21%)和甘露糖(12%)以及脂肪酸肉豆蔻酸(48%)和棕榈酸(52%)是T. foetus总糖脂的组成成分。5. 总糖脂被分离:半乳糖脑苷和神经节苷被鉴定。
{"title":"Polysaccharide and glycolipid composition in Tritrichomonas foetus.","authors":"B P Dias Filho, C S Alviano, W de Souza, J Angluster","doi":"10.1016/0020-711x(88)90360-6","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90360-6","url":null,"abstract":"<p><p>1. The polysaccharide and glycolipid composition in Tritrichomonas foetus was studied by paper, thin-layer and gas-liquid chromatographic analysis. 2. The carbohydrate components of the polysaccharide were glucose (47%), galactose (34%) and mannose (19%). N-acetylneuraminic acid was the sialic acid derivative characterized in the flagellate whole cells. 3. The sialic acid density was estimated as 2.7 x 10(7) residues/cell. 4. The long-chain base dihydrosphingosine, the carbohydrates galactose (67%), glucose (21%) and mannose (12%) as well as the fatty acids myristic (48%) and palmitic (52%) acids were characterized as components of the total glycolipids of T. foetus. 5. Total glycolipids were fractionated: a galactocerebroside and a ganglioside were identified.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90360-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481976","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90357-6
N Bargoni, O Tazartes
1. In chicken embryo cartilage putrescine levels, maximal at day 8, fall by day 16 to a four-fold lower value, which remains unchanged through hatching and in the 12-day-old chick. 2. Spermine and spermidine, initially higher than putrescine, are almost halved between days 8 and 11, and remain constant afterwards. 3. Ornithine decarboxylase is down to 20% of the day 8 value by day 16, and is further reduced in the newly hatched chick. 4. S-Adenosyl-methionine decarboxylase activity shows a 50% reduction between days 8 and 11, and no further changes. 5. Spermidine acetyltransferase activity at day 11 is 30% lower than at day 8, goes back up to the initial level by day 16, and progressively decreases through hatching and the first 12 days of life.
1. 鸡胚软骨腐胺含量在第8天达到最大值,到第16天下降到原来的四分之一,并在整个孵化过程和12日龄的鸡中保持不变。2. 精胺和亚精胺最初比腐胺高,在第8天和第11天之间几乎减半,之后保持不变。3.到第16天,鸟氨酸脱羧酶下降到第8天的20%,并且在新孵化的小鸡中进一步降低。4. s -腺苷-蛋氨酸脱羧酶活性在第8天至第11天下降了50%,并且没有进一步的变化。5. 第11天亚精胺乙酰转移酶活性比第8天降低30%,到第16天恢复到初始水平,并在孵化和出生后12天逐渐降低。
{"title":"Polyamines and enzymes of polyamines metabolism in the cartilage during embryonic development.","authors":"N Bargoni, O Tazartes","doi":"10.1016/0020-711x(88)90357-6","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90357-6","url":null,"abstract":"<p><p>1. In chicken embryo cartilage putrescine levels, maximal at day 8, fall by day 16 to a four-fold lower value, which remains unchanged through hatching and in the 12-day-old chick. 2. Spermine and spermidine, initially higher than putrescine, are almost halved between days 8 and 11, and remain constant afterwards. 3. Ornithine decarboxylase is down to 20% of the day 8 value by day 16, and is further reduced in the newly hatched chick. 4. S-Adenosyl-methionine decarboxylase activity shows a 50% reduction between days 8 and 11, and no further changes. 5. Spermidine acetyltransferase activity at day 11 is 30% lower than at day 8, goes back up to the initial level by day 16, and progressively decreases through hatching and the first 12 days of life.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90357-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481973","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90361-8
F J Joubert
1. Cytotoxin homologues S3C2 and S4C8 from Aspidelaps scutatus were purified by gel filtration and ion exchange chromatography. 2. They consist of 63 amino acids including eight half-cystines. The toxicities of S3C2 and S4C8 were determined and LD50 values of 6.6 and 9.4 micrograms/g mouse were, respectively, found. 3. The complete primary structures of toxins S3C2 and S4C8 have been determined. The two toxins resemble the cytotoxin type toxins and in the cytotoxin homologues the ten structurally invariant amino acids of the neurotoxins and the cytotoxins are conserved.
{"title":"Snake venom toxins--II. The primary structures of cytotoxin homologues S3C2 and S4C8 from Aspidelaps scutatus (shield or shield-nose snake) venom.","authors":"F J Joubert","doi":"10.1016/0020-711x(88)90361-8","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90361-8","url":null,"abstract":"<p><p>1. Cytotoxin homologues S3C2 and S4C8 from Aspidelaps scutatus were purified by gel filtration and ion exchange chromatography. 2. They consist of 63 amino acids including eight half-cystines. The toxicities of S3C2 and S4C8 were determined and LD50 values of 6.6 and 9.4 micrograms/g mouse were, respectively, found. 3. The complete primary structures of toxins S3C2 and S4C8 have been determined. The two toxins resemble the cytotoxin type toxins and in the cytotoxin homologues the ten structurally invariant amino acids of the neurotoxins and the cytotoxins are conserved.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90361-8","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14481977","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90354-0
J T Brozinick, V K Patel, G L Dohm
1. The effect of exercise (2 hr treadmill running at 28 m/min) on PDHa (the activity of the active form of pyruvate dehydrogenase) in untrained rats, trained rats (2 hr/d at 25 m/min for 4 wk), and in 24 hr fasted rats was determined. 2. Exercise increased PDHa activity approximately 2 fold in fed-untrained rats. 3. Fasting decreased PDHa activity in sedentary rats to approximately half the activity in fed rats. 4. The increase in PDHa activity during exercise was less in fasted than fed rats. 5. Training did not change the total activity of PDH (phosphorylated plus nonphosphorylated forms) but the percent of PDH in the active form was increased in muscle of trained-rested rats. 6. PDHa activity was unchanged by acute exercise (2.5 hr at 40 m/min) in the trained rats.
{"title":"Effects of fasting and training on pyruvate dehydrogenase activation during exercise.","authors":"J T Brozinick, V K Patel, G L Dohm","doi":"10.1016/0020-711x(88)90354-0","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90354-0","url":null,"abstract":"<p><p>1. The effect of exercise (2 hr treadmill running at 28 m/min) on PDHa (the activity of the active form of pyruvate dehydrogenase) in untrained rats, trained rats (2 hr/d at 25 m/min for 4 wk), and in 24 hr fasted rats was determined. 2. Exercise increased PDHa activity approximately 2 fold in fed-untrained rats. 3. Fasting decreased PDHa activity in sedentary rats to approximately half the activity in fed rats. 4. The increase in PDHa activity during exercise was less in fasted than fed rats. 5. Training did not change the total activity of PDH (phosphorylated plus nonphosphorylated forms) but the percent of PDH in the active form was increased in muscle of trained-rested rats. 6. PDHa activity was unchanged by acute exercise (2.5 hr at 40 m/min) in the trained rats.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90354-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14482761","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90353-9
K C Abel, S Rattigan, M G Clark
1. alpha- and beta-Adrenergic agonists as well as insulin stimulate 3-O-methyl-D-glucose efflux by the perfused rat heart and increase D-glucose inhibitable cytochalasin B binding by isolated sarcolemma. 2. alpha- and beta-Agonists like insulin increase Vmax for 3-O-methyl-D-glucose efflux and increase Bmax for cytochalasin B binding. 3. The effects of alpha- and beta-agonists are totally Ca2+-dependent whilst those of insulin appear to be only partly Ca2+-dependent.
1. -和-肾上腺素能激动剂以及胰岛素刺激灌注大鼠心脏的3- o -甲基- d -葡萄糖外排,并增加d -葡萄糖抑制细胞松弛素B与分离的肌膜的结合。2. -和-激动剂如胰岛素增加3- o -甲基- d -葡萄糖外排的Vmax和增加细胞松弛素B结合的Bmax。3.α和β激动剂的作用完全依赖于Ca2+,而胰岛素的作用似乎只是部分依赖于Ca2+。
{"title":"Comparison of adrenergic agonist and insulin effects on 3-O-methyl-D-glucose efflux and sarcolemmal cytochalasin B binding by perfused rat heart.","authors":"K C Abel, S Rattigan, M G Clark","doi":"10.1016/0020-711x(88)90353-9","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90353-9","url":null,"abstract":"<p><p>1. alpha- and beta-Adrenergic agonists as well as insulin stimulate 3-O-methyl-D-glucose efflux by the perfused rat heart and increase D-glucose inhibitable cytochalasin B binding by isolated sarcolemma. 2. alpha- and beta-Agonists like insulin increase Vmax for 3-O-methyl-D-glucose efflux and increase Bmax for cytochalasin B binding. 3. The effects of alpha- and beta-agonists are totally Ca2+-dependent whilst those of insulin appear to be only partly Ca2+-dependent.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90353-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"14030514","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 1988-01-01DOI: 10.1016/0020-711x(88)90352-7
T N Tulenko, J L Rabinowitz, R H Cox, W P Santamore
1. We evaluated the influence of cigarette smoking on arterial wall membranes, using Na+-K+-ATPase activity, free cholesterol (FC) and phospholipid (PL) contents as indices of membrane structural and functional integrity. 2. Segments of aorta, carotid and femoral arteries were obtained from normal dogs (controls) and dogs subjected to chronic cigarette smoking for 2 yr (12 cigarettes a day). 3. Na+-K+-ATPase activity was assessed in segments of carotid and femoral arteries using a ouabain-sensitive 86Rb uptake procedure for intact tissues. 4. Free cholesterol and phospholipids were separated, identified, and quantitated from extracts of aortic samples by means of two dimensional thin-layer chromatography. 5. Na+-K+-ATPase activity was reduced in the smoker group in both carotid and femoral arteries. This reduced enzyme activity was accompanied by a rise in cell Na+ levels at both arterial sites. 6. Aortic FC was elevated and the PL profile was altered in the smoker group; as a result, phosphatidylcholine was reduced, whereas lysophosphatidylcholine, phosphatidic acid, and cardiolipin were elevated. 7. Phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine and sphingolipid levels were unchanged. In addition, the FC/PL ratio was increased in the smokers. 8. Taken together, the changes in Na+-K+-ATPase activity, FC/PL ratio and phospholipid profiles observed are consistent with the hypothesis that chronic cigarette smoking causes a reorganization of the phospholipid bilayer in the smooth-muscle cell membrane of the arterial wall.
{"title":"Altered Na+-K+-ATPase, cell Na+ and lipid profiles in canine arterial wall with chronic cigarette smoking.","authors":"T N Tulenko, J L Rabinowitz, R H Cox, W P Santamore","doi":"10.1016/0020-711x(88)90352-7","DOIUrl":"https://doi.org/10.1016/0020-711x(88)90352-7","url":null,"abstract":"<p><p>1. We evaluated the influence of cigarette smoking on arterial wall membranes, using Na+-K+-ATPase activity, free cholesterol (FC) and phospholipid (PL) contents as indices of membrane structural and functional integrity. 2. Segments of aorta, carotid and femoral arteries were obtained from normal dogs (controls) and dogs subjected to chronic cigarette smoking for 2 yr (12 cigarettes a day). 3. Na+-K+-ATPase activity was assessed in segments of carotid and femoral arteries using a ouabain-sensitive 86Rb uptake procedure for intact tissues. 4. Free cholesterol and phospholipids were separated, identified, and quantitated from extracts of aortic samples by means of two dimensional thin-layer chromatography. 5. Na+-K+-ATPase activity was reduced in the smoker group in both carotid and femoral arteries. This reduced enzyme activity was accompanied by a rise in cell Na+ levels at both arterial sites. 6. Aortic FC was elevated and the PL profile was altered in the smoker group; as a result, phosphatidylcholine was reduced, whereas lysophosphatidylcholine, phosphatidic acid, and cardiolipin were elevated. 7. Phosphatidylethanolamine, phosphatidylinositol, phosphatidylserine and sphingolipid levels were unchanged. In addition, the FC/PL ratio was increased in the smokers. 8. Taken together, the changes in Na+-K+-ATPase activity, FC/PL ratio and phospholipid profiles observed are consistent with the hypothesis that chronic cigarette smoking causes a reorganization of the phospholipid bilayer in the smooth-muscle cell membrane of the arterial wall.</p>","PeriodicalId":22539,"journal":{"name":"The International journal of biochemistry","volume":null,"pages":null},"PeriodicalIF":0.0,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0020-711x(88)90352-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13971073","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}