Salinity-sensitive alkaline phosphatase activity in gills of the blue crab, Callinectes sapidus Rathbun

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry Pub Date : 1994-09-01 DOI:10.1016/0305-0491(94)90153-8

Donald L. Lovett , David W. Towle , Jason E. Faris

{"title":"Salinity-sensitive alkaline phosphatase activity in gills of the blue crab, Callinectes sapidus Rathbun","authors":"Donald L. Lovett , David W. Towle , Jason E. Faris","doi":"10.1016/0305-0491(94)90153-8","DOIUrl":null,"url":null,"abstract":"<div>A levamisole-sensitive (Ki = 0.72 mM) alkaline phosphatase (pH optimum 9.1) and a levamisole-insensitive alkaline phosphatase (pH optimum 7.1) are present in gills of the blue crab Callinectes sapidus. Both enzymes are distinct from ouabain-sensitive ATPase. Specific activity for either phosphatase is greatest in the acinar tissue, which lines the branchial vessels. Histochemical localization of the enzymes confirmed this distribution. Activity of levamisole-sensitive alkaline phosphatase is affected by acclimation salinity. Vmax of the levamisole-sensitive alkaline phosphatase is greater in high-salinity crabs than in low-salinity crabs; apparent Km is not significantly different. The levamisole-sensitive alkaline phosphatase associated with the acinar tissue lining the branchial vessels may modulate the osmoregulatory response in blue crabs.</div>","PeriodicalId":100294,"journal":{"name":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","volume":"109 1","pages":"Pages 163-173"},"PeriodicalIF":0.0000,"publicationDate":"1994-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0305-0491(94)90153-8","citationCount":"48","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Comparative Biochemistry and Physiology Part B: Comparative Biochemistry","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0305049194901538","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}

引用次数: 48

Abstract

A levamisole-sensitive (K_i = 0.72 mM) alkaline phosphatase (pH optimum 9.1) and a levamisole-insensitive alkaline phosphatase (pH optimum 7.1) are present in gills of the blue crab Callinectes sapidus. Both enzymes are distinct from ouabain-sensitive ATPase. Specific activity for either phosphatase is greatest in the acinar tissue, which lines the branchial vessels. Histochemical localization of the enzymes confirmed this distribution. Activity of levamisole-sensitive alkaline phosphatase is affected by acclimation salinity. V_max of the levamisole-sensitive alkaline phosphatase is greater in high-salinity crabs than in low-salinity crabs; apparent K_m is not significantly different. The levamisole-sensitive alkaline phosphatase associated with the acinar tissue lining the branchial vessels may modulate the osmoregulatory response in blue crabs.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

蓝蟹鳃中盐敏碱性磷酸酶活性的研究

蓝蟹鳃中存在一种左旋咪唑敏感碱性磷酸酶(Ki = 0.72 mM) (pH最适9.1)和一种左旋咪唑不敏感碱性磷酸酶(pH最适7.1)。这两种酶都不同于缬草碱敏感的atp酶。这两种磷酸酶的特异性活性在排列在鳃裂血管上的腺泡组织中最高。酶的组织化学定位证实了这种分布。驯化盐度对左旋咪唑敏感碱性磷酸酶活性的影响。高盐度蟹的左旋咪唑敏感碱性磷酸酶Vmax大于低盐度蟹;表观Km无显著差异。与鳃血管内腺泡组织相关的左旋咪唑敏感碱性磷酸酶可能调节蓝蟹的渗透调节反应。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文去求助

来源期刊

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry

自引率

0.00%

发文量