CONFORMATION OF BLOOD-GROUP AND VIRUS RECEPTOR GLYCOPROTEINS FROM RED CELLS AND SECRETIONS

被引：31

作者：

JIRGENSO.B

SPRINGER, GF

机构：

[1] Department of Biochemistry, University of Texas, M.D. Anderson Hospital and Tumor Institute, Houston

[2] Department of Immunochemistry Research, Evanston Hospital, Northwestern University, Evanston

来源：

SCIENCE | 1968年 / 162卷 / 3851期

关键词：

D O I：

10.1126/science.162.3851.365

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Optical rotatory dispersion of human blood-group and virus receptor glycoproteins from erythrocytes and secretions was studied in the far-ultraviolet. Erythrocyte membrane blood-group glycoproteins, with potent virus receptor activities, contained significant alpha-helical and extended beta conformations, whereas the glycoproteins of secretions were largely disordered. These conclusions were supported by determination of the Moffitt constants (b0) and by measurements of circular dichroism.

引用

页码：365 / &

共 18 条

[1] CIRCULAR DICHROSIM OF BIOLOGICAL MACROMOLECULES [J].