Oguri S, Nagata Y
Department of Bioresources Chemistry, Faculty of Horticulture, Chiba University, Matsudo, Japan.
Biosci Biotechnol Biochem. 1994 Mar;58(3):507-11. doi: 10.1271/bbb.58.507.
The complete amino acid sequence of a lectin-related 16.5-kDa protein (PCL-RP) isolated from fruit bodies of a lectin-deficient strain of P. cornucopiae is presented. The sequences of six out of the seven peptides generated by digestion with lysylendopeptidase and four of the five peptides generated by cyanogen bromide cleavage were completely analyzed. Overlapping peptides were obtained by arginylendopeptidase digestion. PCL-RP was a single-chain protein consisting of 144 amino acid residues and its N-terminal serine was blocked with acetate. A proline-rich sequence was found in the carboxyl terminal portion. The N-terminal sequence of PCL-RP showed some homology with those of two known Basidiomycete lectins.
本文展示了从一种缺乏凝集素的鬼笔鹅膏菌株子实体中分离出的一种与凝集素相关的16.5 kDa蛋白质（PCL-RP）的完整氨基酸序列。对赖氨酰内肽酶消化产生的七个肽段中的六个以及溴化氰裂解产生的五个肽段中的四个进行了完整序列分析。通过精氨酰内肽酶消化获得了重叠肽段。PCL-RP是一种由144个氨基酸残基组成的单链蛋白质，其N端丝氨酸被乙酰化封闭。在羧基末端部分发现了一个富含脯氨酸的序列。PCL-RP的N端序列与两种已知担子菌凝集素的N端序列有一些同源性。
