title: cDNA cloning, purification and properties of Paralithodes camtschatica metalloprotease.
abstract: Hepatopancreas of king crab Paralithodes camtschatica produces a metalloprotease, which belongs to the astacin family, as cDNA cloning and sequencing showed. The metalloprotease has been purified chromatographically to apparent homogeneity. The purification factor was 16 and activity recovery was 20%. pH and temperature optimum have been determined. In its properties (molecular weight, pI, metal content) the metalloprotease is close to crayfish astacin. However, analysis of the enzyme sequences revealed differences, which account for differences in substrate specificities and imply a different activation mechanism.
authors.affiliation: Chemistry Department of Moscow State University, Leninskie Gory, GSP-3, Moscow, 119899, Russia.
authors.forename: Svetlana A
authors.initials: SA
authors.lastname: Semenova
authors.forename: Galina N
authors.initials: GN
authors.lastname: Rudenskaya
authors.forename: Denis V
authors.initials: DV
authors.lastname: Rebrikov
authors.forename: Vyacheslav A
authors.initials: VA
authors.lastname: Isaev
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D033381:Anomura / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics / Q000302:isolation & purification; D045726:Metalloproteases / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
chemical_list: D018076:DNA, Complementary; D045726:Metalloproteases