Redman D G
Biochem J. 1976 Apr 1;155(1):193-5. doi: 10.1042/bj1550193.
The 24 residues of the N-terminal CNBr peptide from a wheat albumin, that lacks phenylalanine and histidine, have been sequenced. Three of the assignments were made partly by analogy with two other proteins, as evidence is presented that all three proteins are probably identical in this region. Extra evidence for the sequences of the alpha-chymotryptic peptides derived from the N-terminal CNBr peptides of the three proteins, and also for their assembly, has been deposited as Supplementary Publication SUP 50063 (11 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms given in Biochem J. (1976) 153, 5. The nature of such evidence is stated in the text of this present communication.
已对一种缺乏苯丙氨酸和组氨酸的小麦白蛋白的N端溴化氰肽的24个残基进行了测序。其中三个序列的确定部分是通过与其他两种蛋白质进行类比得出的，因为有证据表明这三种蛋白质在该区域可能是相同的。关于这三种蛋白质的N端溴化氰肽衍生的α-胰凝乳蛋白酶肽的序列及其组装的额外证据，已作为补充出版物SUP 50063（11页）存放在英国西约克郡韦瑟比波士顿温泉市英国国家图书馆出借部，邮编LS23 7BQ，可按《生物化学杂志》（1976年）第153卷第5期所述条件从该处获取副本。本文中说明了此类证据的性质。
