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《CHINESE JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY》 1999-02
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Purification and Molecular Structure Analysis of the Time interval Protein Esterase A4 from Diapausing Eggs of Silkworm, Bombyx mori

XU Shiqing 1) ,KAI Hidenori 2) ,XU Junliang 3) ,HIGASI Genitino 2) ,TANI Naoiki 2) ,ZHENG Biping 1) ( 1) School of Sericulture,Suzhou University,Suzhou 215151; 2) Faculty of Agricultural,Tottri University,Koyam  
The Esterase A4(Ease A4) of Bombyx silkworm eggs is a kind of time interval measuring enzyme for resumption of embryonic development in it.The silkworm diapausing eggs of C108 were degreased with acetone,heat treatment at 85℃ and gel filtration through Sephadex G 25,then concentrated and separated with Centricon 10 and Sep Pak C18.At last,they were separated 2 times with HPLC on a YMC Protein RP column.After that,11 8 μg Ease A4 protein was obtained from 10 g silkworm eggs,with high purity appraised by SDS PAGE and matrix assisted laser desorption ionization mass spectrometry (MALDIMS).The amino acid sequence of Ease A4 was analyzed useing the purified enzyme protein from C108 Bombyx silkworm eggs 2 days after oviposition.It is composed of 155 amino acid residues from His to Tyr,and the Mr is 16 601.A glycoside combining at 22 nd amino acid Asn(Asn X Thr)was found in the protein,and the Mr was 740.The bond of S S between the 61 st amino acid residue Cys and 150 th Cys was confirmed.The glycoside and the bond of S S in Ease A4 related to purification and activation of the protein.
【CateGory Index】: Q71
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