MOLECULAR-WEIGHTS OF GLYCOSYLATED AND NONGLYCOSYLATED FORMS OF RECOMBINANT HUMAN STEM-CELL FACTOR DETERMINED BY LOW-ANGLE LASER-LIGHT SCATTERING

被引：41

作者：

ARAKAWA, T ^{[1
]}

LANGLEY, KE ^{[1
]}

KAMEYAMA, K ^{[1
]}

TAKAGI, T ^{[1
]}

机构：

[1] INST PROT RES, SUITA, OSAKA, JAPAN

来源：

ANALYTICAL BIOCHEMISTRY | 1992年 / 203卷 / 01期

关键词：

D O I：

10.1016/0003-2697(92)90042-6

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The molecular weight of recombinant human stem cell factor (SCF) was determined using a low-angle laser light scattering combined with a differential refractometer and a uv detector. The protein samples were applied to these detectors through a gel filtration column by a high-performance liquid chromatographic pump. The Chinese hamster ovary (CHO) cell-derived SCF gave a molecular weight of 53,000 for the entire molecule and 35,000 for the protein moiety only at pH 7.0, indicating that the CHO cell-derived protein is glycosylated by 34%. Since the molecular weight of the polypeptide is 18,600, the results demonstrate that the CHO cell-derived SCF forms a dimer. The molecular weight of Escherichia coli-derived SCF was determined to be 39,000, similar to the above value (35,000). Essentially identical molecular weights were obtained at pH 3.0, indicating no dissociation of the dimer. © 1992.

引用

页码：53 / 57

页数：5

共 28 条

[1] MOLECULAR-CLONING OF MAST-CELL GROWTH-FACTOR, A HEMATOPOIETIN THAT IS ACTIVE IN BOTH MEMBRANE-BOUND AND SOLUBLE FORMS [J].