Inaba K, Akazome Y, Morisawa M
Misaki Marine Biological Station, Faculty of Science, University of Tokyo, Kanagawa, Japan.
Biochem Biophys Res Commun. 1992 Jan 31;182(2):667-74. doi: 10.1016/0006-291x(92)91784-n.
Two-types of high molecular mass proteases have been purified from sea urchin sperm using DEAE-Sephacel, hydroxylapatite and Superdex 200 column chromatography. Both proteases showed similar hydrolyzing activities toward synthetic peptides, but they differed in the molecular mass and peptide composition. One was probably identical to a proteasome (multicatalytic proteinase), judging from its molecular mass (650 kDa) and polypeptide composition. The other one was composed of several polypeptides with molecular masses ranging from 24 kDa to 125 kDa and its molecular mass was estimated as 950 kDa by gel filtration. These two proteases, however, were closely related to each other. Immunological studies revealed that the 950-kDa protease comprised at least five subunits of the 650-kDa protease.
利用DEAE-葡聚糖凝胶、羟基磷灰石和Superdex 200柱层析法,从海胆精子中纯化出了两种高分子量蛋白酶。两种蛋白酶对合成肽均表现出相似的水解活性,但它们的分子量和肽组成有所不同。从其分子量(650 kDa)和多肽组成判断,其中一种可能与蛋白酶体(多催化蛋白酶)相同。另一种由分子量在24 kDa至125 kDa之间的几种多肽组成,通过凝胶过滤法估计其分子量为950 kDa。然而,这两种蛋白酶彼此密切相关。免疫学研究表明,950 kDa的蛋白酶至少包含650 kDa蛋白酶的五个亚基。