Subunit structure of pig kidney cathepsin A.
The two forms of pig kidney cathepsin A (A,L and A,S) were found to be composed of three kinds of polypeptides as common structural subunits with molecular weights of 20,000, 25,000, and 55,000. [32P]-DFP was incorporated into the subunit with a molecular weight of 25,000. This subunit seems to be a catalytic one, on which active serine is present. A subunit composition ratio of 1 : 1 : 1 in native cathepsin A,S was estimated by its molecular weight and those of the subunits. Native cathepsin, A,L also seems to have a subunit composition ratio of 1 : 1 : 1. These results suggest a monomer-polymer relationship between both enzymes.
D000818:Animals; D001665:Binding Sites; D001704:Biopolymers; D002268:Carboxypeptidases; D043402:Cathepsin A; D002403:Cathepsins; D055598:Chemical Phenomena; D002621:Chemistry; D007531:Isoflurophate / Q000378:metabolism; D007668:Kidney / Q000201:enzymology; D008970:Molecular Weight; D013552:Swine
D001704:Biopolymers; D007531:Isoflurophate; D002268:Carboxypeptidases; D002403:Cathepsins; D043402:Cathepsin A