Abstract
The resistance of anti-A-agglutinins from the albumin gland of snails (Helix pomatia) toward enzymic proteolysis led to the discovery of the albumin gland proteinase inhibitor. This inhibitor is different in molecular size and inhibitory and other properties from the epidermal trypsin-kallikrein inhibitors and is present only in the albumin gland. It has not yet been studied as intensively as the low-molecular-weight inhibitors. This chapter examines the assay procedure inhibition of the tryptic hydrolysis of benzoyl-DL-arginine p-nitroanilide (BAPA) is measured by the change in absorbance at 405 nm as described in a previous volume of this treatise. It details the eight-point purification procedure. Properties such as stability, purity, physical properties, specificity, kinetic properties, immunogenic properties, reactive site, distribution and composition have also been detailed.
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