Studies on the multiple forms of aminopeptidase A in bovine seminal vesicle secretion |
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| Authors: | Y Agrawal T Vanha-Perttula |
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| Affiliation: | 1. Department of Animal Biotechnology, Kyungpook National University, Sangju, Gyeongsangbuk-do, 37224, Republic of Korea;2. Department of Animal Science & Technology, Chung-Ang University, Anseong, Gyeonggi-Do, 17546, Republic of Korea;1. Key Laboratory for Animal Genetics, Breeding, Reproduction and Molecular Design, College of Animal Science and Technology, Yangzhou University, Yangzhou 225009, China;2. Joint International Research Laboratory of Agriculture & Agri-Product Safety, the Ministry of Education of China, Yangzhou University, Yangzhou, Jiangsu 225009, China;1. Inherent Biosciences, Salt Lake City, Utah;2. Division of Population Health Research, Division of Intramural Research, Eunice Kennedy Shriver National Institute of Child Health and Human Development, Bethesda, Maryland;3. Department of Cell Biology and Physiology, Brigham Young University, Provo, Utah;4. Division of Urology, Department of Surgery, University of Utah School of Medicine, Salt Lake City, Utah |
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| Abstract: | After gel filtration, anion exchange chromatography and chromatofocusing aminopeptidase A (AP-A) of bovine seminal vesicle secretion (VS-S) was found to exist in multiple forms. Depending on the pH used (pH 6.5-8.5) gel filtration of VS-S revealed 1-3 forms of AP-A. At pH 8.5 two dissimilar low-molecular-weight forms of AP-A converted into aggregated high-molecular-weight form. The aggregated AP-A was dissociated into an intermediate form with Triton X-100 and/or sodium deoxycholate and further into two low-molecular-weight forms with thiol compounds and neuraminidase. The aggregated, intermediate and low-molecular-weight forms of AP-A displayed some differences in catalytic properties, modifier characteristics and thermal inhibition. |
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