[The study of the metal-binding region in human growth hormone using immobilized metal ion affinity gel-electrophoresis].
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 Affinity Gel-electrophoresis (IMAG). The mutant hormones, composed of polypeptide chain segments of the human and porcine growth hormones, lacked His18, which may be crucial for binding of the intact hormone to the transition metal ions. The mutations did not affect the affinity of human growth hormone to immobilized zinc ions; the structural analysis implied that the human growth hormone contains two IDA-Zn(II) potential sorption sites formed by amino acid residues His21, Asp171, and Glu174 and/or His18 and Glu174.
Anisimova
M V
MV
Bioengineering Center, Russian Academy of Sciences, pr. 60-letya Oktyabrya 7/1, Moscow, 117312 Russia.
Shul'ga
A A
AA
Levichkin
I V
IV
Kirpichnikov
M P
MP
Poliakov
K M
KM
Skriabin
K G
KG
Vijayalakshmi
M A
MA
Varlamov
V P
VP
D000818:Animals; D001665:Binding Sites; D004586:Electrophoresis; D013006:Growth Hormone / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008670:Metals / Q000737:chemistry* / Q000378:metabolism; D009154:Mutation; D011485:Protein Binding
D008670:Metals; D013006:Growth Hormone