Sequence homologies between p36, the substrate of pp60src tyrosine kinase and a 67 kDa protein isolated from bovine aorta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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Sequence homologies between p36, the substrate of pp60src tyrosine kinase and a 67 kDa protein isolated from bovine aorta

Authors:	F Martin J Derancourt J P Capony S Colote J C Cavadore

Institution:	1. Geo Constech Pvt. Ltd., New Delhi, India;2. Department of Earth Sciences, Indian Institute of Technology Bombay, Powai, Mumbai 400076, Maharashtra, India;1. Department of Social Science, Shanghai University of Engineering Science, China;2. Department of Economics, McMaster University, Canada;1. State Key Laboratory of Ocean Engineering, Shanghai Jiao Tong University, Shanghai 200240, PR China;2. Center for Environmental Energy Engineering, University of Maryland, College Park, MD 20742, USA;1. U.S. Centers for Disease Control and Prevention, Atlanta, USA;2. Institute of Public Health, Tirana, Albania;3. Levin and Morgan, Bethesda, USA;4. Task Force for Global Health, Atlanta, USA

Abstract:	A 67 kDa actin-binding protein was isolated from bovine aorta. Partial amino acid sequence determination of two large thermolysin peptides were used to compare 67 kDa bovine aorta protein and p36 the substrate of pp60src tyrosine kinase. Sequence analysis shows that 67 kDa bovine aorta protein shares common domains with p36 and possesses the consensus aminoacid sequences of mammalian Ca2+-dependent membrane-binding protein and p36/gelsolin.

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