TRYPSIN ACTIVATION OF ENTERO-TOXIN FROM CLOSTRIDIUM-PERFRINGENS TYPE-A - FRAGMENTATION AND SOME PHYSICOCHEMICAL PROPERTIES
TRYPSIN ACTIVATION OF ENTERO-TOXIN FROM CLOSTRIDIUM-PERFRINGENS TYPE-A - FRAGMENTATION AND SOME PHYSICOCHEMICAL PROPERTIES
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DOI：
10.1016/0005-2795(81)90165-3
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发表时间：
1981-01-01
期刊：
影响因子：
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通讯作者：
SKJELKVALE, R
中科院分区：
文献类型：
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作者：
GRANUM, PE;WHITAKER, JR;SKJELKVALE, R
C.通过用胰蛋白酶处理，A型产气荚膜杆菌肠毒素被活化约3倍，而没有观察到MW的变化。在8 M尿素中变性后，胰蛋白酶化的肠毒素失去了约4000道尔顿的小肽。肠毒素的单半胱氨酸残基与9个脯氨酸残基中的7个一起位于小肽中。胰蛋白酶活化，而不去除的小肽，增加了外部的氨基数目从8至11。胰蛋白酶处理肠毒素没有改变蛋白质的抗原特性。甘氨酸是天然肠毒素的C-末端残基，而丹磺酰基α- N-末端的氨基酸不能被鉴定。
C. perfringens type A enterotoxin was activated about 3-fold by treatment with trypsin, without an observed change in MW. On denaturation in 8 M urea, the trypsinated enterotoxin lost a small peptide of about 4000 daltons. The single cysteine residue of enterotoxin was in the small peptide together with 7 of 9 residues of proline. Trypsin activation, without removal of the small peptide, increased the outside number of amino groups from 8 to 11. The trypsin treatment of the enterotoxin did not change the antigenic properties of the protein. Glycine was the C-terminal residue of the native enterotoxin while the dansyl .alpha.-amino acid of the N-terminal could not be identified.