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球形红假单胞菌中结晶3-羟基丁酸脱氢酶的纯化及性质

Purification and properties of crystalline 3-hydroxybutyrate dehydrogenase from Rhodopseudomonas spheroides.

作者信息

Bergmeyer H U, Gawehn K, Klotzsch H, Krebs H A, Williamson D H

出版信息

Biochem J. 1967 Feb;102(2):423-31. doi: 10.1042/bj1020423.

DOI:10.1042/bj1020423
PMID:4291491
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1270263/
Abstract
  1. The purification and crystallization of 3-hydroxybutyrate dehydrogenase from extracts of Rhodopseudomonas spheroides is described. 2. The molecular weight was calculated to be 85000 by sedimentation equilibrium. 3. Although the enzyme is stable at 0-4 degrees , dilute solutions are rapidly inactivated at 37 degrees ; NADH(2) or Ca(2+) ions prevent this inactivation. 4. The enzyme is extremely sensitive to mercurials, but can be protected by NADH(2) or Ca(2+) ions. 5. From studies on p-hydroxymercuribenzoate binding it is estimated that the enzyme contains 5-6 moles of rapidly reacting thiol groups/mole. 6. d-Lactate and dl-2-hydroxybutyrate are competitive inhibitors of d-3-hydroxybutyrate oxidation. 7. The properties of the crystalline enzyme are compared with those of 3-hydroxybutyrate dehydrogenase preparations from other sources.
摘要
  1. 描述了从球形红假单胞菌提取物中纯化和结晶3-羟基丁酸脱氢酶的过程。2. 通过沉降平衡计算,分子量为85000。3. 尽管该酶在0-4摄氏度时稳定,但稀溶液在37摄氏度时会迅速失活;NADH(2)或Ca(2+)离子可防止这种失活。4. 该酶对汞剂极为敏感,但可被NADH(2)或Ca(2+)离子保护。5. 通过对对羟基汞苯甲酸结合的研究估计,该酶每摩尔含有5-6摩尔快速反应的巯基。6. d-乳酸和dl-2-羟基丁酸是d-3-羟基丁酸氧化的竞争性抑制剂。7. 将结晶酶的性质与其他来源的3-羟基丁酸脱氢酶制剂的性质进行了比较。
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6b3/1270263/0fb287d05dd8/biochemj00746-0051-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6b3/1270263/0fb287d05dd8/biochemj00746-0051-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a6b3/1270263/0fb287d05dd8/biochemj00746-0051-a.jpg

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