Hory / D, Weder J K
Z Lebensm Unters Forsch. 1976 Dec 31;162(4):349-56. doi: 10.1007/BF01122787.
The sequences of amino acid residues at the amino and carboxyl terminus and around the reactive sites of the trypsin chymotrypsin inhibitor PCI 3 from the seeds of runner beans (Phaseolus coccineus L.) were estimated by aminopeptidase O and carbosypeptidase A degradation before and after enzymatical modification with trypsin or chymotrypsin. Beginning at the amino terminus the sequences are :Ser-Glu-Ala-Gly-Gln-...,...-Ile-Tyr-Lys-Ser-Gln-(Pro)-...with Lys-Ser as reactive site against trypsin, ...-Asp-Val-Ala-Leu-Ser-(Pro)-...with Leu-Ser as reactive site against alpha-chymotrypsin, and ...-Thr-Arg-Ala-Lys-Phe-Leu as C-terminus. The importance of the serine residue in the reactive sites concerning the specificity of inhibitors is discussed.
通过用胰蛋白酶或糜蛋白酶进行酶促修饰前后,利用氨肽酶O和羧肽酶A降解法,对来自菜豆(Phaseolus coccineus L.)种子的胰蛋白酶-糜蛋白酶抑制剂PCI 3的氨基和羧基末端以及活性位点周围的氨基酸残基序列进行了测定。从氨基末端开始,序列为:Ser-Glu-Ala-Gly-Gln-...,...-Ile-Tyr-Lys-Ser-Gln-(Pro)-...,其中Lys-Ser为针对胰蛋白酶的活性位点,...-Asp-Val-Ala-Leu-Ser-(Pro)-...,其中Leu-Ser为针对α-糜蛋白酶的活性位点,以及...-Thr-Arg-Ala-Lys-Phe-Leu作为羧基末端。讨论了活性位点中的丝氨酸残基对于抑制剂特异性的重要性。