PURIFICATION AND PARTIAL AMINO-ACID-SEQUENCE OF INITIATORIN, A PROSTATIC ENDOPEPTIDASE OF THE SILKWORM, BOMBYX-MORI
PURIFICATION AND PARTIAL AMINO-ACID-SEQUENCE OF INITIATORIN, A PROSTATIC ENDOPEPTIDASE OF THE SILKWORM, BOMBYX-MORI
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DOI：
10.1016/0965-1748(94)90134-1
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发表时间：
1994-12-01
影响因子：
3.8
通讯作者：
OSANAI, M
中科院分区：
文献类型：
--
作者：
AIGAKI, T;KASUGA, H;OSANAI, M
我们已经纯化了启动素，一种前列腺内肽酶，在家蚕的精囊中启动蛋白质-精氨酸降解级联。通过测定BAEE （N α -苯甲酰- l-精氨酸乙酯）水解活性来监测该酶从精子囊中纯化的情况。精子囊被用作这种酶的来源。在几种同工异构体中，主要形式（MW, 29 kDa）被纯化超过200倍。启动子n端序列与丝氨酸型内肽酶具有较强的同源性。
We have purified initiatorin, a prostatic endopeptidase that initiates the protein-arginine degradation cascade in the spermatophore of Bombyx mori. Purification of the enzyme from spermatophores was monitored by measuring BAEE (N alpha-benzoyl-L-arginine-ethyl ester) hydrolyzing activity. Spermatophores were used as a source for this enzyme. Of several isoforms the major form (MW, 29 kDa) was purified over 200-fold. The N-terminal sequence of initiatorin showed strong homology with those of serine-type of endopeptidases.