SPECIFICITY OF THE COLLAGENASE FROM THE INSECT HYPODERMA-LINEATUM
SPECIFICITY OF THE COLLAGENASE FROM THE INSECT HYPODERMA-LINEATUM
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DOI：
10.1111/j.1432-1033.1985.tb09171.x
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发表时间：
1985-01-01
期刊：
影响因子：
--
通讯作者：
KEIL, B
中科院分区：
文献类型：
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作者：
LECROISEY, A;KEIL, B
结果表明，该酶具有特异性。lineatum是一种与胰蛋白酶相关的丝氨酸蛋白酶，已经通过使用天然胶原和非胶原底物进行了研究。在25度。C和中性pH值的降解胶原蛋白的幼虫酶在溶液中的结果在52%的损失比粘度，而没有损失的螺旋度。消化物的片段长间距微晶的电子显微镜显示条带41和44之间的一个裂解区域的发生，而Edman降解指示该区域中的几个裂解位点。皮皮胶原酶不同于来自螃蟹Uca pugilator的蛋白酶I和II，其催化胶原分子的多个区域中的裂解，也不同于脊椎动物胶原酶，其仅裂解残基775和776之间的胶原。除了对胶原蛋白的特异性作用外，皮皮属胶原酶降解胰岛素的氧化链B;主要裂解发生在Leu 15-Tyr 16键处，随后在Arg 22-Gly 23和Lys 29-Ala 30键处发生两次较小裂解。幼虫酶对胰蛋白酶或糜蛋白酶的合成肽底物无作用。
Specificity of the collagenase from the larvae H. lineatum, a serine protease related to trypsin, has been investigated by using native collagen and non-collageneous substrates. At 25.degree. 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 Leu15-Tyr16 bond followed by two minor cleavages at the Arg22-Gly23 and Lys29-Ala30 bonds. The larval enzyme has no action on synthetic peptide substrates of trypsin or chymotrypsin.