Kim W S, Hatsuzawa K, Ishizuka Y, Hashiba K, Murakami K, Nakayama K
Institute of Applied Biochemistry, University of Tsukuba, Ibaraki, Japan.
J Biol Chem. 1990 Apr 15;265(11):5930-3.
Renin is produced from an inactive precursor, prorenin, through proteolytic cleavage at paired basic amino acid residues. In this study, an enzyme which specifically cleaves mouse Ren 2 prorenin at the paired basic residues has been purified from mouse submandibular gland by CM-Toyopearl chromatography, antipain-Sepharose chromatography, and isoelectric focusing. This enzyme, named prorenin converting enzyme, consists of two polypeptide chains of 17 and 10 kDa. The enzyme has an isoelectric point of 9.5-9.8, and its pH optimum is between 7.5 and 8.5. It specifically cleaves the peptide bond on the carboxyl side of the Arg at the Lys-Arg pair of mouse Ren 2 prorenin to yield mature renin but does not cleave mouse Ren 1 and human prorenins. Studies on the effects of inhibitors indicate that this enzyme is a serine protease that differs from the enzymes processing other prohormones at paired basic amino acid residues.
肾素由无活性的前体——肾素原，通过在成对碱性氨基酸残基处的蛋白水解切割产生。在本研究中，一种能在成对碱性残基处特异性切割小鼠Ren 2肾素原的酶，已通过CM - Toyopearl层析、抗蛋白酶 - 琼脂糖层析和等电聚焦从小鼠下颌下腺中纯化出来。这种酶被命名为肾素原转化酶，由两条分别为17 kDa和10 kDa的多肽链组成。该酶的等电点为9.5 - 9.8，最适pH在7.5至8.5之间。它特异性切割小鼠Ren 2肾素原赖氨酸 - 精氨酸对中精氨酸羧基侧的肽键，产生成熟肾素，但不切割小鼠Ren 1和人肾素原。抑制剂作用研究表明，这种酶是一种丝氨酸蛋白酶，与在成对碱性氨基酸残基处加工其他激素原的酶不同。
