Expression of growth hormone-releasing factor analog Leu27GRF(1–44)OH in Escherichia coli: Purification and characterization of the expressed protein
- 1 May 1991
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 286 (2) , 638-644
- https://doi.org/10.1016/0003-9861(91)90093-x
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- System for High-Level Production in Escherichia coli and Rapid Purification of Recombinant Proteins: Application to Epitope Mapping, Preparation of Antibodies, and Structure—Function AnalysisPublished by Elsevier ,1990
- Gene synthesis, E. coli expression and purification of the bovine growth hormone releasing factor analog, (Leu27,Hse45) bGRFJournal of Biotechnology, 1989
- Genetic Approach to Facilitate Purification of Recombinant Proteins with a Novel Metal Chelate AdsorbentNature Biotechnology, 1988
- New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residuesJournal of Chromatography A, 1987
- Solution structure of human growth hormone releasing factorJournal of Molecular Biology, 1986
- Production and Characterization of Growth Hormone Releasing Factor Analogs Through Recombinant DNA and Chemical TechniquesNature Biotechnology, 1986
- Chapter 19. Growth Hormone Releasing Factors (Somatocrinins)Published by Elsevier ,1985
- A rapid, sensitive method for detection of alkaline phosphatase-conjugated anti-antibody on Western blotsAnalytical Biochemistry, 1984
- Protein and cell membrane iodinations with a sparingly soluble chloroamide, 1,3,4,6-tetrachloro-3a,6a-diphenylglycolurilBiochemical and Biophysical Research Communications, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970