The amino acid sequence of bovine growth hormone.

Facultad de Farmacia y Bioquímica, Departamento de Química Biológica y Centro para el Estudio de las Hormonas Hipofisarias, Junín 956, Buenos Aires, Argentina
FEBS letters (Impact Factor: 3.54). 09/1971; 16(3):198-200. DOI: 10.1016/0014-5793(71)80132-1
Source: PubMed
  • [Show abstract] [Hide abstract]
    ABSTRACT: Reactivity of histidines in bovine growth hormone towards ethoxyformic anhydride was investigated and localization in the molecule of two kinetically distinguishable classes was achieved, a slow class including only histidine residue 169 (k = 0.180 min-1) and a fast one composed of histidines 19 and 21 (k = 0.900 min-1). Total ethoxyformylation of bovine growth hormone brought about a complete loss of its capacity to compete with 125I-labelled hormone for rat-liver binding sites, but modification of approximately half of the fast histidine group was enough to produce an important decrease in this capacity. Circular dichroism studies indicated no significant changes in protein conformation with all three histidine residues modified. Practically full binding capacity was restored when these residues were regenerated by treatment with hydroxylamine. These results suggest that one or both of the fast reacting histidine residues are involved in bovine growth hormone binding to its specific receptors.
    International journal of peptide and protein research 05/1983; 21(4):451-7.
  • [Show abstract] [Hide abstract]
    ABSTRACT: A nonapeptide, Arg-Glu-Leu-Glu-Asp-Gly-Thr-Pro-Arg, corresponding to the 123–131 sequence of bovine pituitary growth hormone, was prepared by a modified solid phase synthesis. To avoid an acid- or base-catalysed rearrangement at the Asp-Gly bond, which gives rise to an aspartimide-containing peptide, a new combination of protecting groups was introduced. The 2-(4-biphenylyl)-2-propyloxycarbonyl group was used for Nα-protection, a t-butyl ester for the β-carboxyl of aspartic acid, and a p-alkoxybenzyl alcohol ester for the anchoring bond to the resin support. The nonapeptide showed growth hormone activity in the hypophysectomized rat tibia epiphyseal width test, but was inactive in the hypophysectomized rat body weight gain test.
    International journal of peptide and protein research 02/1974; 6(2):103-9.
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: Growth Hormone (GH) gene is a member of gene family through the evolutionary process from a small common ancestral gene by a series of gene duplications. The role of the GH in growth and performance controls has been extensively studied in human, mice and livestock. Many researchers have considered GH as a strong candidate gene for evaluation of genetic polymorphisms that could be associated with economic traits in cattle. We report here a novel missense mutation within the exon 5 of the bovine Growth Hormone (bGH) gene. We could amplified 522 bp fragments from eight unrelated Hanwoo cattle by PCR, then, subsequently cloned and sequenced. An Msp I RFLP corresponding to a C to T transition was observed at position 2258 nt. From this result, we could predict a missense mutation (Arg to Trp) at codon 166 in a highly conserved region among many mammals. Codominant Mendelian segregation of the two alleles, Msp I (+) and Msp I (-), was observed in two full-sib F2 families (n = 32, African taurine Bos taurus African zebu Bos indicus) and eight half-sib Hanwoo families. For the availability of genetic marker, we have performed PCR-RFLP with a large number of individual animals from 15 different cattle breeds (European and Asian taurines, and African indicines). Consideration of breed frequencies of Msp I (-) allele in relation to breed type and their geographic origins, shows higher frequencies in humped breeds or Asian cattle breeds than in humpless or European breeds. This result indicates that the missense mutation can be contributed the functional significance such as the signal transduction through the receptor binding, also may be used as a marker for selection of the economic traits in Hanwoo.
    Journal of Animal Science and Technology. 01/2003; 45(1).


Available from