{"title":"In vitro activity of five antifungal agents against Malassezia pachydermatis.","authors":"Y Uchida, T Nakade, K Kitazawa","doi":"10.1292/jvms1939.52.851","DOIUrl":"https://doi.org/10.1292/jvms1939.52.851","url":null,"abstract":"","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"851-3"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.851","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13538817","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}
M Yamada, M Yukawa, K Mochizuki, H Sekikawa, M Kenmotsu
{"title":"Sarcocystis in Murray Grey stock cattle introduced from Australia.","authors":"M Yamada, M Yukawa, K Mochizuki, H Sekikawa, M Kenmotsu","doi":"10.1292/jvms1939.52.883","DOIUrl":"https://doi.org/10.1292/jvms1939.52.883","url":null,"abstract":"","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"883-5"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.883","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13272847","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}
Chuzan virus at 2 to 3 passage levels in cell cultures after isolation was inoculated intravenously into 15 seronegative pregnant cows at 89 to 150 days of gestation. All of the cows developed viremia a few days after inoculation and antibodies 2 weeks after inoculation. No clinical signs, except leukopenia, were observed throughout the experimental period. These 15 cows delivered 15 calves after normal gestation. One of the calves which was born to a dam inoculated at 120 days of gestation, showed impairment of movement, and the remaining 14 were healthy. Postmortem examination revealed that this calf had hydranencephaly- cerebellar hypoplasia (HCH) syndrome and that the remaining calves were normal. Two of the 15 calves, including the one that had HCH syndrome, had antibody to Chuzan virus in their precolostral sera. These findings provide additional evidence that Chuzan virus is the etiological agent of an epizootic of congenital abnormalities with HCH syndrome of calves in Japan, 1985 to 1986. We propose to name the HCH syndrome caused by Chuzan virus infection Chuzan disease.
{"title":"Hydranencephaly-cerebellar hypoplasia in a newborn calf after infection of its dam with Chuzan virus.","authors":"Y Miura, M Kubo, Y Goto, Y Kono","doi":"10.1292/jvms1939.52.689","DOIUrl":"https://doi.org/10.1292/jvms1939.52.689","url":null,"abstract":"<p><p>Chuzan virus at 2 to 3 passage levels in cell cultures after isolation was inoculated intravenously into 15 seronegative pregnant cows at 89 to 150 days of gestation. All of the cows developed viremia a few days after inoculation and antibodies 2 weeks after inoculation. No clinical signs, except leukopenia, were observed throughout the experimental period. These 15 cows delivered 15 calves after normal gestation. One of the calves which was born to a dam inoculated at 120 days of gestation, showed impairment of movement, and the remaining 14 were healthy. Postmortem examination revealed that this calf had hydranencephaly- cerebellar hypoplasia (HCH) syndrome and that the remaining calves were normal. Two of the 15 calves, including the one that had HCH syndrome, had antibody to Chuzan virus in their precolostral sera. These findings provide additional evidence that Chuzan virus is the etiological agent of an epizootic of congenital abnormalities with HCH syndrome of calves in Japan, 1985 to 1986. We propose to name the HCH syndrome caused by Chuzan virus infection Chuzan disease.</p>","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"689-94"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.689","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13321369","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}
Characteristics of CPE produced by porcine enteroviruses (PEV) were examined by Immunoperoxidase (IP) staining method. Viral antigens were detected earlier than appearance of CPE. Distinctive characteristics of the three CPE types were clearly showed by the method. In cross reactions by IP staining, the titers of the staining were high (1:6,400 to 1:25,600), even though neutralizing titers of PEV with CPE II or III were low (1:200 to 1:400). The very close relationship was detected between PEV with the same CPE type, but the very low relationships were detected between PEV with the different CPE type. The relationships in CPE I group were various. The results by IP staining were more relative to CPE type than the serotype. Thus, IP staining is one method to classify PEV clearly.
{"title":"Relation of serological- and CPE- classification of porcine enteroviruses to the classification by immunoperoxidase (IP) staining, and observation of CPE by IP staining method.","authors":"E Honda, I Watanabe, K Okazaki, T Kumagai","doi":"10.1292/jvms1939.52.795","DOIUrl":"https://doi.org/10.1292/jvms1939.52.795","url":null,"abstract":"<p><p>Characteristics of CPE produced by porcine enteroviruses (PEV) were examined by Immunoperoxidase (IP) staining method. Viral antigens were detected earlier than appearance of CPE. Distinctive characteristics of the three CPE types were clearly showed by the method. In cross reactions by IP staining, the titers of the staining were high (1:6,400 to 1:25,600), even though neutralizing titers of PEV with CPE II or III were low (1:200 to 1:400). The very close relationship was detected between PEV with the same CPE type, but the very low relationships were detected between PEV with the different CPE type. The relationships in CPE I group were various. The results by IP staining were more relative to CPE type than the serotype. Thus, IP staining is one method to classify PEV clearly.</p>","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"795-800"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.795","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"12861782","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}
T Tsutsui, I Murao, E Kawakami, A Ogasa, G H Stabenfeldt
In order to better understand androgen secretion in the tom cat during the breeding season, observations of diurnal changes in peripheral blood testosterone (T) levels, were made and the relation between androgen levels (androstenedione (A), 5 alpha-dihydrotestosterone (DHT). T) in testicular and peripheral vein blood was borne. Histologic examinations of the testis were also performed to investigate spermatogenic function. The 9 tom cats used in these studies were 2-3 years old, weighed 3.5-4.0 kg, and were raised in a room under natural lighting. As a result, diurnal peripheral blood T levels in the tom cat fluctuated greatly according to each individual, but since no definite trend could be identified, secretion was determined to be episodic. Although fairly large differences in the 3 types of androgen were observed in testicular vein blood depending on the individual animal, levels on the left and right were almost equal. Moreover, a correlation was found between the testicular and peripheral vein blood concentrations of the 3 androgens (A: p less than 0.01; DHT: p less than 0.05; T: p less than 0.01). Therefore, secretion of testicular androgen can be inferred by measuring peripheral blood androgen levels. Testicular histological examination revealed active spermatogenesis in all of the cats, and no significant inter individual differences were detected in either seminiferous tubule diameters or any of the various germ cells.
为了更好地了解繁殖季节猫猫的雄激素分泌情况,我们观察了猫猫外周血睾酮(T)水平的日变化以及雄激素(雄烯二酮(A)、5 α -二氢睾酮(DHT)水平之间的关系。T)在睾丸和外周静脉血液中携带。还进行了睾丸组织学检查以研究生精功能。在这些研究中使用的9只猫猫年龄为2-3岁,体重为3.5-4.0公斤,在自然光下的房间里饲养。结果,猫猫的日外周血T水平在每个个体之间波动很大,但由于没有确定的趋势,因此确定分泌是偶发性的。虽然在睾丸静脉血液中观察到的三种雄激素有很大的差异,这取决于个体动物,但左右两侧的水平几乎相等。3种雄激素在睾丸和外周静脉血中浓度呈显著相关(a: p < 0.01;DHT: p < 0.05;T: p < 0.01)。因此,睾丸雄激素的分泌可以通过测量外周血雄激素水平来推测。睾丸组织学检查显示,所有猫的精子发生都很活跃,在精管直径和各种生殖细胞中均未发现显著的个体差异。
{"title":"Androgen concentration in the blood and spermatogenic function of tom cats during the breeding season.","authors":"T Tsutsui, I Murao, E Kawakami, A Ogasa, G H Stabenfeldt","doi":"10.1292/jvms1939.52.801","DOIUrl":"https://doi.org/10.1292/jvms1939.52.801","url":null,"abstract":"<p><p>In order to better understand androgen secretion in the tom cat during the breeding season, observations of diurnal changes in peripheral blood testosterone (T) levels, were made and the relation between androgen levels (androstenedione (A), 5 alpha-dihydrotestosterone (DHT). T) in testicular and peripheral vein blood was borne. Histologic examinations of the testis were also performed to investigate spermatogenic function. The 9 tom cats used in these studies were 2-3 years old, weighed 3.5-4.0 kg, and were raised in a room under natural lighting. As a result, diurnal peripheral blood T levels in the tom cat fluctuated greatly according to each individual, but since no definite trend could be identified, secretion was determined to be episodic. Although fairly large differences in the 3 types of androgen were observed in testicular vein blood depending on the individual animal, levels on the left and right were almost equal. Moreover, a correlation was found between the testicular and peripheral vein blood concentrations of the 3 androgens (A: p less than 0.01; DHT: p less than 0.05; T: p less than 0.01). Therefore, secretion of testicular androgen can be inferred by measuring peripheral blood androgen levels. Testicular histological examination revealed active spermatogenesis in all of the cats, and no significant inter individual differences were detected in either seminiferous tubule diameters or any of the various germ cells.</p>","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"801-6"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.801","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13538811","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}
{"title":"Isolation and observation of the phenotype of feline fourth component of complement.","authors":"T Furukawa, F Sugiyama","doi":"10.1292/jvms1939.52.843","DOIUrl":"https://doi.org/10.1292/jvms1939.52.843","url":null,"abstract":"","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"843-6"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.843","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13538815","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}
K Ono, K Inui, T Hasegawa, N Matsuki, H Watanabe, S Takagi, A Hasegawa, I Tomoda
The change in activities of 3 major antioxidative enzymes in equine erythrocytes, superoxide dismutase (SOD), glutathione peroxidase (GSHpx), and catalase, was investigated in order to evaluate the effect of exercise. Blood samples were obtained from 11 thoroughbred horses before and immediately after vigorous exercise which induced the increase of plasma lipid peroxide (Lpx) concentration from 1.16 +/- 0.40 nmol/ml to 1.29 +/- 0.34 nmol/ml. Following the exercise, the GSHpx activity in erythrocytes was significantly reduced from 69 +/- 10 IU/gHb to 65 +/- 8 IU/gHb, whereas SOD and catalase activities were not changed. Effects of an antioxidative compound, containing selenium and vitamin E(Se-E), on the response of antioxidative enzyme activities following the exercise were examined. Seven horses were injected intramuscularly with Se-E(Se:25 mg, vitamin E:54.8 mg) and received the same vigorous exercise. After Se-E treatment, plasma Lpx levels before the exercise were decreased from 1.24 +/- 0.09 nmol/ml to 0.86 +/- 0.03 nmol/ml, however, SOD, GSHpx, and catalase activities were not varied. The Se-E treatment slightly prevented the decrease in GSHpx activity and the increase in plasma Lpx level after the exercise, having no effect on SOD and catalase activities. These results suggested that the changes of GSHpx activity in erythrocytes might reflect the protective condition against exercise-induced lipid peroxidation.
{"title":"The changes of antioxidative enzyme activities in equine erythrocytes following exercise.","authors":"K Ono, K Inui, T Hasegawa, N Matsuki, H Watanabe, S Takagi, A Hasegawa, I Tomoda","doi":"10.1292/jvms1939.52.759","DOIUrl":"https://doi.org/10.1292/jvms1939.52.759","url":null,"abstract":"<p><p>The change in activities of 3 major antioxidative enzymes in equine erythrocytes, superoxide dismutase (SOD), glutathione peroxidase (GSHpx), and catalase, was investigated in order to evaluate the effect of exercise. Blood samples were obtained from 11 thoroughbred horses before and immediately after vigorous exercise which induced the increase of plasma lipid peroxide (Lpx) concentration from 1.16 +/- 0.40 nmol/ml to 1.29 +/- 0.34 nmol/ml. Following the exercise, the GSHpx activity in erythrocytes was significantly reduced from 69 +/- 10 IU/gHb to 65 +/- 8 IU/gHb, whereas SOD and catalase activities were not changed. Effects of an antioxidative compound, containing selenium and vitamin E(Se-E), on the response of antioxidative enzyme activities following the exercise were examined. Seven horses were injected intramuscularly with Se-E(Se:25 mg, vitamin E:54.8 mg) and received the same vigorous exercise. After Se-E treatment, plasma Lpx levels before the exercise were decreased from 1.24 +/- 0.09 nmol/ml to 0.86 +/- 0.03 nmol/ml, however, SOD, GSHpx, and catalase activities were not varied. The Se-E treatment slightly prevented the decrease in GSHpx activity and the increase in plasma Lpx level after the exercise, having no effect on SOD and catalase activities. These results suggested that the changes of GSHpx activity in erythrocytes might reflect the protective condition against exercise-induced lipid peroxidation.</p>","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"759-65"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.759","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13539714","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}
A low molecular weight protein was separated from urine samples obtained from a heifer with spontaneous renal disease and from cows with CaNa2EDTA-induced renal dysfunction. The molecular weight and electrophoretic mobility of the separated protein were examined. The low molecular weight protein collected by gel filtration chromatography was further separated into two fractions by ion exchange chromatography using DEAE-cellulose. One of the two fractions, the lowest molecular weight protein showed a single band in SDS-PAGE, and its molecular weight was approximately 12,000. An antiserum against this protein formed a single precipitin line with the urine from cows with experimentally induced renal dysfunction and a heifer with spontaneous renal disease by the double immunodiffusion technique. However, the antiserum did not form any precipitin line with the concentrated urine of healthy cow and human beta 2-microglobulin. In cellulose acetate membrane electrophoresis, this protein migrated in the same position as that of serum gamma-globulin from healthy cow.
{"title":"Isolation and purification of a low molecular weight protein from bovine urine.","authors":"S Kawamura, H Inoue, T Oda, N Itoh, S Higuchi","doi":"10.1292/jvms1939.52.787","DOIUrl":"https://doi.org/10.1292/jvms1939.52.787","url":null,"abstract":"<p><p>A low molecular weight protein was separated from urine samples obtained from a heifer with spontaneous renal disease and from cows with CaNa2EDTA-induced renal dysfunction. The molecular weight and electrophoretic mobility of the separated protein were examined. The low molecular weight protein collected by gel filtration chromatography was further separated into two fractions by ion exchange chromatography using DEAE-cellulose. One of the two fractions, the lowest molecular weight protein showed a single band in SDS-PAGE, and its molecular weight was approximately 12,000. An antiserum against this protein formed a single precipitin line with the urine from cows with experimentally induced renal dysfunction and a heifer with spontaneous renal disease by the double immunodiffusion technique. However, the antiserum did not form any precipitin line with the concentrated urine of healthy cow and human beta 2-microglobulin. In cellulose acetate membrane electrophoresis, this protein migrated in the same position as that of serum gamma-globulin from healthy cow.</p>","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"787-93"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.787","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13539717","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}
H Nakayama, M Morozumi, J K Kang, K Uchida, N Goto
{"title":"Hepatic nodular fibrosis in a dog.","authors":"H Nakayama, M Morozumi, J K Kang, K Uchida, N Goto","doi":"10.1292/jvms1939.52.831","DOIUrl":"https://doi.org/10.1292/jvms1939.52.831","url":null,"abstract":"","PeriodicalId":19620,"journal":{"name":"Nihon juigaku zasshi. The Japanese journal of veterinary science","volume":"52 4","pages":"831-3"},"PeriodicalIF":0.0,"publicationDate":"1990-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1292/jvms1939.52.831","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13538814","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}