Degradation of cystathionine gamma-lyase in rat liver lysosomes: effect of leupeptin treatment.
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.
D000818:Animals; D003542:Cystathionine gamma-Lyase / Q000378:metabolism*; D015151:Immunoblotting; D007976:Leupeptins / Q000494:pharmacology*; D008099:Liver / Q000187:drug effects* / Q000201:enzymology; D008247:Lysosomes / Q000187:drug effects* / Q000201:enzymology; D008970:Molecular Weight; D051381:Rats; D012016:Reference Values
D007976:Leupeptins; D003542:Cystathionine gamma-Lyase; C032854:leupeptin