Awata S, Nakayama K, Sato A, Kawamura M, Suzuki I, Sugahara K, Kodama H
Department of Nutritional Biochemistry, Faculty of Food Science, Kochi Gakuen College, Japan.
Biochem Mol Biol Int. 1995 May;35(6):1183-7.
Highly purified lysosomes from the livers of normal and leupeptin-treated rats were subjected to immunoblot analysis, using antibodies against rat liver cystathionine gamma-lyase. Normal lysosomes showed small amount of single band at about 40 kDa, whereas the leupeptin-treated lysosomes showed large amounts of a major band at about 40 kDa and a minor band at about 35 kDa. These observations suggest that cystathionine gamma-lyase is sequestered into lysosomes at the original subunit molecular weight and is degraded in the lysosome by way of the sequential formation of an intermediate with distinct molecular weight.
使用抗大鼠肝脏胱硫醚γ-裂解酶的抗体,对来自正常大鼠和经亮抑酶肽处理的大鼠肝脏的高度纯化溶酶体进行免疫印迹分析。正常溶酶体在约40 kDa处显示少量单一条带,而经亮抑酶肽处理的溶酶体在约40 kDa处显示大量主要条带,在约35 kDa处显示少量次要条带。这些观察结果表明,胱硫醚γ-裂解酶以原始亚基分子量被隔离到溶酶体中,并通过依次形成具有不同分子量的中间体在溶酶体中降解。