Isolation and partial characterization of prochymosin and chymosin from cat.
Extracts of cat gastric mucosa contain a zymogen that after activation shows partial immunochemical identity with chymosin (EC 3.4.23.4) from calf. Cat prochymosin has been purified by column chromatography and gel filtration, and cat chymosin was obtained after acid activation of the zymogen. The enzyme showed the optimum of general proteolytic activity at pH 2.5. The amino acid compositions of cat prochymosin and chymosin were similar to those of the corresponding proteins from calf. The first 27 residues of both cat prochymosin and chymosin have been sequenced. Among these 54 positions only 13 differences have been observed between the proteins from cat and calf. The results support the hypothesis that the chymosins form a group of neonatal gastric proteases with high milk-clotting activity, but with such weak general proteolytic activity that postnatal uptake of IgG is not hindered.
D000595:Amino Acid Sequence; D000818:Animals; D000831:Animals, Newborn / Q000378:metabolism; D002415:Cats; D002417:Cattle; D002845:Chromatography; D012085:Chymosin / Q000302:isolation & purification / Q000378:metabolism*; D004789:Enzyme Activation; D005753:Gastric Mucosa / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007122:Immunoelectrophoresis; D008892:Milk / Q000378:metabolism; D008970:Molecular Weight
D012085:Chymosin