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• W2022274063 abstract "1. A high mol. wt proteinase inhibitor has been purified from the haemolymph of the freshwater crayfish Astacus astacus. 2. The protein is a disulphide-bonded dimer (Mr 390,000) of two identical polypeptide chains (Mr 185,000). 3. The inhibitor displays a broad specificity and protects trypsin from inhibition by soybean trypsin inhibitor and thus is similar to vertebrate α2-macroglobulin. 4. The α2-macroglobulin-like inhibitor from Astacus interacts with bovine trypsin in an equimolar stoichiometry thereby decreasing tryptic hydrolysis of N-benzoyl-l-arginine-ethylester to 50% residual activity. In contrast, the activity of Astacus protease, a digestive zinc proteinase from crayfish toward succinyl-alanyl-alanyl-alanyl-4-nitroanilide is inhibited almost completely. 4. Sensitivity of the inhibitor to methylamine and autolytic cleavage suggests the presence of an internal thioester bond. 5. The N-terminal amino acid sequence of Astacusα2-macroglobulin is strongly related to the α2-macroglobulins from Pacifastacus leniusculus (91% identity) and from the lobster Homarus americanus (72% identity). In contrast, only 25% of the residues are identical with the α2-macroglobulin from the horseshoe crab Limulus polyphemus. There is also a faint similarity to human complement protein C3 and human α2-macroglobulin." @default.
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• W2022274063 date "1991-01-01" @default.
• W2022274063 modified "2023-10-03" @default.
• W2022274063 title "α2-macroglobulin from the haemolymph of the freshwater crayfish Astacus astacus" @default.
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• W2022274063 doi "https://doi.org/10.1016/0305-0491(91)90244-8" @default.
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