The study of the metal-binding region in human growth hormone using immobilized metal ion affinity gel-electrophoresis

Authors
Anisimova, MV Shulga, AA Levichkin, IV Kirpichnikov, MP Polyakov, KM Skryabin, KG Vijayalakshmi, MA Varlamov, VP
Citation
Mv. Anisimova et al., The study of the metal-binding region in human growth hormone using immobilized metal ion affinity gel-electrophoresis, RUS J BIOOR, 27(1), 2001, pp. 23-26
Citations number
16
Categorie Soggetti
Chemistry & Analysis
Journal title
RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
ISSN journal
10681620 → ACNP
Volume
27
Issue
1
Year of publication
2001
Pages
23 - 26
Database
ISI
SICI code
1068-1620(200101/02)27:1<23:TSOTMR>2.0.ZU;2-G
Abstract
The zinc(II)-binding affinities of recombinant human growth hormone and two its mutants, 14-33 and 14-95, were studied using Immobilized Metal Ion Aff inity Gel-electrophoresis (IMAG). The mutant hormones, composed of polypept ide chain segments of the human and porcine growth hormones, lacked His18, which may be crucial for binding of the intact hormone to the transition me tal ions. The mutations did not affect the affinity of human growth hormone to immobilized zinc ions. the structural analysis implied that the human g rowth hormone contains two IDA-Zn(II) potential sorption sites formed by am ino acid residues His21, Asp171, and Glu174 and/or His18 and Glu174.