Acylation and carbamylation of equine muscle carbonic anhydrase (CA-III) upon reaction with p-nitrophenyl esters and carbamoyl phosphate期刊界 All Journals 搜尽天下杂志传播学术成果专业期刊搜索期刊信息化学术搜索

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Acylation and carbamylation of equine muscle carbonic anhydrase (CA-III) upon reaction with p-nitrophenyl esters and carbamoyl phosphate

Authors:	T Nishita H F Deutsch

Institution:	1. Center for Built Environment, The Built Environment Department, Sungkyunkwan University, Suwon, 440-746, Republic of Korea;2. Dept. of Water Resources, Graduate School of Water Resources, Sungkyunkwan University, Suwon, 440-746, Republic of Korea;1. Medical Biology Research Center, Kermanshah University of Medical Sciences, Kermanshah, Iran;2. Department of Biology, Faculty of Science, Razi University, Kermanshah, Iran;3. Pharmaceutical Sciences Research Center, Faculty of Pharmacy, Kermanshah University of Medical Sciences, Kermanshah, Iran;4. Department of Organic Colorants, Institute for Color Science and Technology, 1668814811 Tehran, Iran;5. Center of Excellence for Color Science and Technology, Institute for Color Science and Technology, 16656118481 Tehran, Iran;6. Department of Pharmacognosy and Biotechnology, Faculty of Pharmacy, Kermanshah University of Medical Sciences, Kermanshah, Iran;1. Atatürk University, Kazim Karabekir Education Faculty, Department of Mathematics and Science Education, Chemistry Laboratory, 25240, Erzurum, Turkey;2. Hassan First University of Settat, Faculty of Sciences and Technologies, Laboratory of Biochemistry, Neurosciences, Natural Resources and Environment, 577, Settat, Morocco;3. Hassan First University of Settat, Faculty of Sciences and Technologies, Laboratory of Applied Chemistry and Environment, 577, Settat, Morocco;4. Atatürk University, Faculty of Health Sciences, Department of Nutrition and Dietetics, 25240, Erzurum, Turkey

Abstract:	Equine muscle carbonic anhydrase (CA-III) behaves like ubiquitin in undergoing extensive acylation of N epsilon-lysine residues upon reacting with p-nitrophenyl esters. The enzyme undergoes extensive carbamoylation of lysine residues when reacted with carbamoyl phosphate. The modification of from 6 to 7 lysine residues results in the production of a series of more anodic electrophoretic components. The derivatization of the lysine residues leads to a marked decrease in the enzyme's ability to hydrate CO2. The equine CA-III possesses both acid and alkaline phosphatase activities in contrast to the rabbit which possesses only the former type.

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