Pub Date : 1963-11-15DOI: 10.1016/0006-3002(63)90907-7
Jose Depaoli , Kristen B. Eik-Nes
In order to determine if the ovarian metabolism of pregnenolone differed between estrus and pregnancy, [7α-3H]pregnenolone was infused by the ovarian artery in anesthetized dogs and steroids containing tritium isolated in ovarian vein blood.
1.
1. Within 5 min the canine ovary metabolized pregnenolone to 17α-hydroxy-pregnenolone, progesterone, 17α-hydroxyprogesterone, dehydroepiandrosterone, androsterone, testosterone and probably estradiol.
2.
2. Induction of mating in the female dog by treatment with human chorionic gonadotropin was associated with a high capacity of the ovary to convert pregnenolone to testosterone and androstenedione.
3.
3. Dogs in the early part of pregnancy metabolized a considerable amount of the infused pregnenolone to progesterone.
{"title":"Metabolism in vivo of [7α-3H]pregnenolone by the dog ovary","authors":"Jose Depaoli , Kristen B. Eik-Nes","doi":"10.1016/0006-3002(63)90907-7","DOIUrl":"10.1016/0006-3002(63)90907-7","url":null,"abstract":"<div><p>In order to determine if the ovarian metabolism of pregnenolone differed between estrus and pregnancy, [7α-<sup>3</sup>H]pregnenolone was infused by the ovarian artery in anesthetized dogs and steroids containing tritium isolated in ovarian vein blood. </p><ul><li><span>1.</span><span><p>1. Within 5 min the canine ovary metabolized pregnenolone to 17α-hydroxy-pregnenolone, progesterone, 17α-hydroxyprogesterone, dehydroepiandrosterone, androsterone, testosterone and probably estradiol.</p></span></li><li><span>2.</span><span><p>2. Induction of mating in the female dog by treatment with human chorionic gonadotropin was associated with a high capacity of the ovary to convert pregnenolone to testosterone and androstenedione.</p></span></li><li><span>3.</span><span><p>3. Dogs in the early part of pregnancy metabolized a considerable amount of the infused pregnenolone to progesterone.</p></span></li></ul></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 457-465"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90907-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670745","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90909-0
Lise Gruen Donovan
Iodination at pH 9.5 has converted three of the six tyrosyl residues of ribonuclease to 3,5-diiodotyrosyl residues. The iodinated ribonuclease is still enzymatically active toward ribonucleic acid. The diiodotyrosyl residues have approximately normal pK's, while the tyrosyl residues remaining have abnormally high pK's. Hence, iodination has taken place on the normal tyrosyl residues.
Two of the iodinated tyrosyl residues have been shown to be No. 115 and No.92; hence, these appear to be normal tyrosyl residues. One of the non-iodinated tyrosyl residues is No. 97, and hence is one of the abnormal tyrosyl residues. The location of the other normal tyrosyl residue (or the other two abnormal ones) remains uncertain.
{"title":"Location of normal and abnormal tyrosyl residues in ribonuclease","authors":"Lise Gruen Donovan","doi":"10.1016/0006-3002(63)90909-0","DOIUrl":"10.1016/0006-3002(63)90909-0","url":null,"abstract":"<div><p>Iodination at pH 9.5 has converted three of the six tyrosyl residues of ribonuclease to 3,5-diiodotyrosyl residues. The iodinated ribonuclease is still enzymatically active toward ribonucleic acid. The diiodotyrosyl residues have approximately normal p<em>K</em>'s, while the tyrosyl residues remaining have abnormally high p<em>K</em>'s. Hence, iodination has taken place on the normal tyrosyl residues.</p><p>Two of the iodinated tyrosyl residues have been shown to be No. 115 and No.92; hence, these appear to be normal tyrosyl residues. One of the non-iodinated tyrosyl residues is No. 97, and hence is one of the abnormal tyrosyl residues. The location of the other normal tyrosyl residue (or the other two abnormal ones) remains uncertain.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 474-491"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90909-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670747","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90905-3
Elaine B. Newman , Boris Magasanik
Cultivation of serine-glycine auxotrophs of Escherichia coli in a medium containing serine and a purine base results in a temporary inability of the cells to grow upon transfer to a medium containing glycine as the nutrilite. It could be shown that this failure to grow is due to the inability of the cells to obtain single-carbon units from glycine. The formation of the enzyme system required for the synthesis of single-carbon units from glycine seems to be controlled through repression exerted by the intracellular single carbons. The intracellular concentration of single-carbon units derived from the β-carbon of serine is apparently increased by the addition of a purine base to the growth medium.
{"title":"The relation of serine-glycine metabolism to the formation of single-carbon units","authors":"Elaine B. Newman , Boris Magasanik","doi":"10.1016/0006-3002(63)90905-3","DOIUrl":"10.1016/0006-3002(63)90905-3","url":null,"abstract":"<div><p>Cultivation of serine-glycine auxotrophs of <em>Escherichia coli</em> in a medium containing serine and a purine base results in a temporary inability of the cells to grow upon transfer to a medium containing glycine as the nutrilite. It could be shown that this failure to grow is due to the inability of the cells to obtain single-carbon units from glycine. The formation of the enzyme system required for the synthesis of single-carbon units from glycine seems to be controlled through repression exerted by the intracellular single carbons. The intracellular concentration of single-carbon units derived from the β-carbon of serine is apparently increased by the addition of a purine base to the growth medium.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 437-448"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90905-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670743","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90914-4
Margaret S. Gibson
{"title":"Production of ethylene by beef heart mitochondria","authors":"Margaret S. Gibson","doi":"10.1016/0006-3002(63)90914-4","DOIUrl":"10.1016/0006-3002(63)90914-4","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 528-530"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90914-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670751","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90918-1
Alexander Pihl, Tore Sanner
{"title":"Protection of sulfhydryl compounds against ionizing radiation","authors":"Alexander Pihl, Tore Sanner","doi":"10.1016/0006-3002(63)90918-1","DOIUrl":"10.1016/0006-3002(63)90918-1","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 537-539"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90918-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23672494","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90923-5
Julia F. De Boiso, A.O.M. Stoppani
{"title":"The biosynthesis of serine in baker's yeast","authors":"Julia F. De Boiso, A.O.M. Stoppani","doi":"10.1016/0006-3002(63)90923-5","DOIUrl":"10.1016/0006-3002(63)90923-5","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 551-553"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90923-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23672498","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90908-9
Herbert H. Wotiz, Barbara S. Ziskind, Ira Ringler
Liver tissue obtained from rats after short-term infusion of [16-14C]estrone was homogenized and differentially fractionated into nuclei, mitochondria, microsomes and supernatant. The greatest amount of radioactivity was found in the supernatant fraction, followed by the nuclei and mitochondria with the lowest amount in the microsomes. The highest specific activity was present in the supernatant fraction followed by the mitochondria and microsomes with the lowest value obtained for the nuclei. Examination of the individual fractions showed probable evidence for binding of estrogen to liver protein, formation of little if any conjugates, possible degradation of ring D and the production of estradiol and another substance more polar than estriol.
{"title":"Studies in steroid metabolism XVII. Intracellular distribution of [16-14C]estrone in rat liver","authors":"Herbert H. Wotiz, Barbara S. Ziskind, Ira Ringler","doi":"10.1016/0006-3002(63)90908-9","DOIUrl":"10.1016/0006-3002(63)90908-9","url":null,"abstract":"<div><p>Liver tissue obtained from rats after short-term infusion of [16-<sup>14</sup>C]estrone was homogenized and differentially fractionated into nuclei, mitochondria, microsomes and supernatant. The greatest amount of radioactivity was found in the supernatant fraction, followed by the nuclei and mitochondria with the lowest amount in the microsomes. The highest specific activity was present in the supernatant fraction followed by the mitochondria and microsomes with the lowest value obtained for the nuclei. Examination of the individual fractions showed probable evidence for binding of estrogen to liver protein, formation of little if any conjugates, possible degradation of ring D and the production of estradiol and another substance more polar than estriol.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 466-473"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90908-9","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670746","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90910-7
D.G. Schmidt, T.A.J. Payens
The preparation of a mixture of the starch-gel components 1.07 and 1.10 of the α-casein family is described. Apart from minor genetical differences these α-caseins appear to be identical. At pH 6.2 and 7.5 the α-caseins strongly associate. At pH 12.2 they dissociate into sub-units of molecular weight 16500 and an axial ratio of 7.5. Arginine is the only N-terminal amino acid.
{"title":"The purification and some properties of a calcium-sensitive α-casein","authors":"D.G. Schmidt, T.A.J. Payens","doi":"10.1016/0006-3002(63)90910-7","DOIUrl":"10.1016/0006-3002(63)90910-7","url":null,"abstract":"<div><p>The preparation of a mixture of the starch-gel components 1.07 and 1.10 of the α-casein family is described. Apart from minor genetical differences these α-caseins appear to be identical. At pH 6.2 and 7.5 the α-caseins strongly associate. At pH 12.2 they dissociate into sub-units of molecular weight 16500 and an axial ratio of 7.5. Arginine is the only N-terminal amino acid.</p></div>","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 492-499"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90910-7","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23670748","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 : 1963-11-15DOI: 10.1016/0006-3002(63)90921-1
Lowell D. Zeleznick , Terrell C. Myers, Edward B. Titchener
{"title":"Growth of Escherichia coli on methyl- and ethylphosphonic acids","authors":"Lowell D. Zeleznick , Terrell C. Myers, Edward B. Titchener","doi":"10.1016/0006-3002(63)90921-1","DOIUrl":"10.1016/0006-3002(63)90921-1","url":null,"abstract":"","PeriodicalId":94301,"journal":{"name":"Biochimica et biophysica acta","volume":"78 3","pages":"Pages 546-547"},"PeriodicalIF":0.0,"publicationDate":"1963-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0006-3002(63)90921-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"23672496","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}
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