Open AccessSpecificity of the collagenase from the insect Hypoderma lineatum
Author(s) -
LECROISEY Anne,
KEIL Borivoj
Publication year - 1985
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1985.tb09171.x
Subject(s) - collagenase , trypsin , serine protease , edman degradation , protease , microbial collagenase , chymotrypsin , cleavage (geology) , biochemistry , enzyme , biology , chemistry , proteases , hemolymph , microbiology and biotechnology , peptide sequence , paleontology , fracture (geology) , gene
Specificity of the collagenase from the larvae Hypoderma lineatum , a serine protease related to trypsin, has been investigated by using native collagen and non‐collageneous substrates. At 25°C and neutral pH the degradation of collagen by the larval enzyme in solution results in a 52% loss of specific viscosity, without loss of helicity. Electron microscopy of segment‐long‐spacing crystallites of the digest shows the occurrence of one cleavage region between bands 41 and 44 whereas Edman degradation indicates several cleavage loci in this region. Hypoderma collagenase differs from proteinases I and II from the crab Uca pugilator , which catalyse cleavages in multiple regions of the collagen molecule, and also from vertebrate collagenases, which cleave collagen only between residues 775 and 776. Apart of specific action on collagen, Hypoderma collagenase degrades the oxidized chain B of insulin; the major cleavage occurs at the Leu 15 ‐Tyr 16 bond followed by two minor cleavages at the Arg 22 ‐Gly 23 and Lys 29 ‐Ala 30 bonds. The larval enzyme has no action on synthetic peptide substrates of trypsin or chymotrypsin.