Studies on the elastolytic activity of chymotrypsin.
Chymotrypsin can completely solubilize insoluble [3H]-labeled ligamentum nuchae elastin. At similar enzyme levels, trypsin solubilizes only 5% of the elastin substrate whereas pancreatic elastase completely solubilizes the elastin at one-tenth the concentration required for chymotrypsin solubilization. The elastolytic activity of chymotrypsin is dependent on Ca+2, is enhanced by SDS, and is inhibited by NaCl at concentrations above 10 mM. The elastolytic activity of chymotrypsin is also inhibited by TPCK, a chymotrypsin specific inhibitor, but not by TLCK, a trypsin specific inhibitor. Neither TPCK nor TLCK abolish the elastolytic activity of pancreatic elastase. The sizes of [3H]elastin fragments produced by the elastolytic activity of chymotrypsin are similar to those produced by pancreatic elastase, and larger than those produced by trypsin.
Collins
J F
JF
Thoman
P J
PJ
Shaw
S L
SL
Fine
R
R
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002417:Cattle; D002918:Chymotrypsin / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004549:Elastin / Q000378:metabolism*; D066298:In Vitro Techniques; D008022:Ligaments / Q000378:metabolism; D010196:Pancreatic Elastase / Q000378:metabolism; D012995:Solubility; D013379:Substrate Specificity; D014107:Tosyllysine Chloromethyl Ketone / Q000494:pharmacology; D014108:Tosylphenylalanyl Chloromethyl Ketone / Q000494:pharmacology; D014357:Trypsin / Q000378:metabolism
D014107:Tosyllysine Chloromethyl Ketone; D014108:Tosylphenylalanyl Chloromethyl Ketone; D004549:Elastin; D002918:Chymotrypsin; D010196:Pancreatic Elastase; D014357:Trypsin; D002118:Calcium