Cheevers W P, Robertson G A, Archer B G, Crawford T B
Intervirology. 1980;14(1):44-9. doi: 10.1159/000149161.
Lactoperoxidase iodination of intact and disrupted equine infectious anemia virus revealed that glycopeptide gp79 is the major surface component of this virus, whereas glycopeptides gp64 and gp40 as well as the principle nonglycosylated structural polypeptides p29 and p13 are internal. Virus 'envelope' particles, banding in isopycnic centrifugation at approximately 1.10 g/cm3, contained the glycopeptides but no internal nonglycosylated proteins. Glycopeptides gp79, gp64 and gp40 and core polypeptide p29 were isolated by SDS-PAGE, iodinated in vitro, and compared by two-dimensional tryptic peptide analysis. Tryptic digests of the glycopeptides were similar but distinct from that of p29.
对完整的和裂解的马传染性贫血病毒进行乳过氧化物酶碘化反应，结果显示糖肽gp79是该病毒的主要表面成分，而糖肽gp64和gp40以及主要的非糖基化结构多肽p29和p13位于病毒内部。在等密度离心时密度约为1.10 g/cm3的病毒“包膜”颗粒含有糖肽，但不含内部非糖基化蛋白。通过SDS-PAGE分离出糖肽gp79、gp64和gp40以及核心多肽p29，进行体外碘化反应，并通过二维胰蛋白酶肽分析进行比较。糖肽的胰蛋白酶消化产物相似，但与p29的不同。
