Arai K, Huss K, Madison J, Putnam F W, Salzano F M, Franco M H, Santos S E, Freitas M J
Department of Biology, Indiana University, Bloomington 47405.
Proc Natl Acad Sci U S A. 1989 Mar;86(6):1821-5. doi: 10.1073/pnas.86.6.1821.
Conventional horizontal starch-gel electrophoresis in four buffer systems and structural studies were performed on four albumin variants, and the findings were compared with similar previous data. Albumins Coari I and Porto Alegre I have a previously unreported amino acid substitution (glutamic acid replaced by lysine at position 358, denoted 358 Glu----Lys). The alteration in albumin Porto Alegre II (501 Glu----Lys) is the same as that found for three alloalbumins of Asiatic origin, designated Vancouver, Birmingham, and Adana. Albumin Oriximiná I has the same exchange as albumin Maku (541 Lys----Glu). Some of these findings can be explained only by the occurrence of independent mutations at the same site in the albumin gene. They also point to a third cluster of mutations in that gene, indicating hypermutability in some of its segments.
在四种缓冲系统中进行了常规水平淀粉凝胶电泳,并对四种白蛋白变体进行了结构研究,然后将研究结果与之前的类似数据进行了比较。白蛋白科阿里I和阿雷格里港I存在一个此前未报道的氨基酸替换(第358位的谷氨酸被赖氨酸取代,记为358 Glu----Lys)。白蛋白阿雷格里港II(501 Glu----Lys)的改变与在三种亚洲起源的同种白蛋白(即温哥华、伯明翰和阿达纳)中发现的改变相同。白蛋白奥里希米纳I与白蛋白马库具有相同的交换(541 Lys----Glu)。其中一些发现只能通过白蛋白基因同一位置发生独立突变来解释。它们还指向该基因中的第三组突变,表明其某些片段具有高突变性。