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血管紧张素转换酶的一般生理生化特性血管紧张素转换酶或血管紧张素Ⅰ转换酶(ACE)又名激肽酶Ⅱ,按系统命名法为肽酰二肽水解酶(EC3.4.15.1)。它是分裂肽链C-端二肽残基的水解酶,首先在马血浆中测得。ACE存在于哺乳动物体内,但也在某些禽类体内发现。它催化血管紧张素Ⅰ水解,使之转换成具有增压作用的血管紧张素Ⅱ。血管紧张素Ⅰ是一种十肽,由肾素催化血清蛋白质前身血管紧张素原水解形成。不同动物体内血管紧张素Ⅰ的氨基酸残基排列次序略有不同,在马血清中其氨基酸残基顺
General Physiological and Biochemical Characteristics of Angiotensin Converting Enzymes Angiotensin converting enzyme or angiotensin I converting enzyme (ACE), also known as kininase II, is peptidyl dipeptide hydrolase (EC3.4.15.1) by the system nomenclature . It is a hydrolase that cleaves the C-terminal dipeptide residues of the peptide chain, first measured in horse plasma. ACE is found in mammals but is also found in some birds. It catalyzes the hydrolysis of angiotensin I, converting it into angiotensin II with a boost. Angiotensin I is a decapeptide that is formed by the hydrolysis of renin-stimulated pro-angiotensin protein. Angiotensin Ⅰ in different animals in vivo amino acid residues arranged in slightly different order, the amino acid residues in horse serum