HUMAN LEUKOCYTE INTERFERON - PRODUCTION, PURIFICATION TO HOMOGENEITY, AND INITIAL CHARACTERIZATION

被引：228

作者：

RUBINSTEIN, M ^{[1
]}

RUBINSTEIN, S ^{[1
]}

FAMILLETTI, PC ^{[1
]}

MILLER, RS ^{[1
]}

WALDMAN, AA ^{[1
]}

PESTKA, S ^{[1
]}

机构：

[1] NEW YORK BLOOD CTR, LINDSLEY F KIMBALL RES INST, NEW YORK, NY 10021 USA

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1979年 / 76卷 / 02期

关键词：

D O I：

10.1073/pnas.76.2.640

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：

A method of fractionating proteins by high-performance liquid partition chromatography has been developed and used for isolation and purification to homogeneity of one of the species of human leukocyte interferon. The homogeneous interferon exhibited a sharp peak on high-performance liquid chromatography and a single narrow band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Extraction of the gel gave a single sharp peak of antiviral activity coinciding with the protein band. The specific activity of pure interferon was found to be 2-4 x 108 units/mg, based on amino acid analysis. The molecular weight is 17,500-18,000.

引用

页码：640 / 644

页数：5

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