OCCURRENCE OF THIOL PROTEINASES IN THE EGGS OF THE SILKWORM, BOMBYX-MORI
OCCURRENCE OF THIOL PROTEINASES IN THE EGGS OF THE SILKWORM, BOMBYX-MORI
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DOI:
10.1093/oxfordjournals.jbchem.a133521
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发表时间:
1981-01-01
影响因子:
2.7
通讯作者:
TAKAHASHI, K
中科院分区:
文献类型:
--
作者:
KAGEYAMA, T;TAKAHASHI, SY;TAKAHASHI, K
In the crude extract of matured eggs of the silkworm (B. mori), proteolytic activity was detected only in the acidic pH region with maximal activity at pH 3.5; this activity was maintained throughout development. No appreciable activity was observed in the neutral to alkaline pH region either in matured eggs or in eggs at early embryonic stages. Two molecular forms of proteinases active at pH 3.5 were obtained from matured eggs, and their MW were estimated to be > 160,000 and .apprx. 68,000, respectively. An additional form of 40,000 MW appeared in eggs just before hatching. They were strongly inhibited by thiol proteinase inhibitors, such as p-chloromercuribenzoate (pCMB), p-chloromercuriphenyl sulfonate (pCMPS) and N-[N-(L-3-trans-carboxyoxirane-2-carbonyl)-L-leucyl]agmatine (E-64); pepstatin, diisopropylphosphorofluoridate, and EDTA were without effect, suggesting that they are thiol enzymes. They hydrolyzed casein, bovine serum albumin, egg albumin and .gamma.-globulin. They could not hydrolyze .alpha.-N-benzoyl-DL-arginine p-nitroanilide, .alpha.-N-benzoyl-DL-arginine .beta.-naphthylamide and several other synthetic substrates. These thiol proteinases differ from hitherto known animal tissue thiol proteinases.