Purification and properties of teleost growth hormone

Farmer, Susan Walker; Papkoff, Harold; Hayáshida, T.; Bewley, Thomas A.; Bern, Howard A.; Li, Choh Hao

doi:10.1016/0016-6480(76)90070-8

Cited by 84 publications

(11 citation statements)

References 40 publications

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“…Using BolTranging between 25 and 30%, the assay was sensitive enough to measure immunoreactive GH in as little as 2 -10 pL gilthead sea bream plasma. The EDs0 (1.5 -2.0 ng/ mL) was comparable to that measured for tilapia (Farmer et al 1976), eel (Kishida and Hirano 1988), and chinook salmon (Le Bail et al 199 1) GH RIAs, and markedly lower than the value reported for carp (Cook et al 1983) and chum salmon (Bolton et al 1986;Wagner and McKeown 1986) assays. Furthermore, the precision of the assay was reasonably-consistent when intia-and inter-assay CVs are considered.…”

Section: Discussionsupporting

confidence: 54%

“…Homologous radioimmunoassays (RIA) for measuring circulating and pituitary GH levels in tilapia (Farmer et al 1976), carp (Cook et al 1983), eel (Kishida and Hirano 1988), and salmonids (Bolton et al 1986;Wagner and McKeown 1986;Le Bail et al 1991) are available. A suitable enzyme immunoassay for oncorhynchid GH has also been developed as an alternative to conventional RIA (Farbridge and Leatherland 1991).…”

Section: Introductionmentioning

confidence: 99%

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Application of a sensitive radioimmunoassay for the measurement of growth hormone in gilthead sea bream (Sparus aurata) and other sparid fish

Bail¹,

Mourot²,

Zohar³

et al. 1993

Can. J. Zool.

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LE BAIL, P.-Y., MOUROT, B., ZOHAR, Y., and P~REZ-SANCHEZ, J. 1993. Application of a sensitive radioimmunoassay for the measurement of growth hormone in gilthead sea bream (Sparus aurata) and other sparid fish. Can. J. Zool. 71: 1500-1505. The development of a homologous radioimmunoassay (RIA) for gilthead sea bream growth hormone (sbGH) is described.RIA sensitivity was 0.4 ng/mL, and ED,, was 1.74 + 0.05 ng/mL. Intra-and inter-assay coefficients of variation were 3.4 and 8.8%, respectively, at ED,, levels. Mammalian growth hormones (GH), carp gonadotropin, chinook salmon gonadotropin, ovine porlactin, and recombinant tilapia prolactin did not show cross-reactivity. Serial dilutions of recombinant trout GH indicated a low but significant cross-reactivity. The displacement curves for plasma and pituitary homogenates from sparid fish (gilthead sea bream, blacktail, white sea bream, Couch's sea bream, and marmor-brassen) were parallel to that of the sbGH standard. Pituitary homogenates from other perciform fish tested (gaper, grey mullet, red mullet, and sea pike) also showed parallel slopes of inhibition. Pituitary homogenates from common sole, sea scorpion, forked hake, goldfish, rainbow trout, and European eel showed low or negligible cross-reactivity. These results suggest that the GHs of perciform fish have a number of similarities in structure. RIA of sea bream GH can be used to quantify the GH of sparid fish and perciform fish, provided a validation has been carried out.

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Section: Discussionsupporting

confidence: 54%

Section: Introductionmentioning

confidence: 99%

Application of a sensitive radioimmunoassay for the measurement of growth hormone in gilthead sea bream (Sparus aurata) and other sparid fish

Bail¹,

Mourot²,

Zohar³

et al. 1993

Can. J. Zool.

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“…Recently, growth hormones from tilapia (9), sturgeon (10), carp (11), and chum salmon (unpublished result) and prolactin from chum salmon (12) were purified. In the case of chum salmon growth hormone, a partial amino acid sequence has been determined (unpublished data).…”

mentioning

confidence: 99%

Cloning and expression of cDNA for salmon growth hormone in Escherichia coli

Sekine

Mizukami

Nishi

et al. 1985

Proc. Natl. Acad. Sci. U.S.A.

167

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ABSTRACTcDNA clones encoding chum salmon (Oncorhynchus keta) growth hormone (sGH) have been isolated from a cDNA library prepared from chum salmon pituitary gland poly(A)+ RNA. Synthetic oligodeoxynucleotide mixtures based on amino acid residues 23-28 of sGH were used as hybridization probes to select recombinant plasmids carrying the sGH coding sequence. The complete nucleotide sequence of sGH cDNA has been determined. The cDNA sequence codes for a polypeptide of 210 amino acids, including a putative signal sequence of 22 amino acids. The 5' and 3' untranslated regions of the message were 64 and 426 bases long, respectively. Mature sGH was efficiently expressed in Escherichia coli carrying a plasmid in which the sGH cDNA was under control of the E. coli trp promoter; sGH comprised about 15% of the total cellular protein in such bacteria. The partially purified sGH from E. coli stimulated the growth of rainbow trout and the activity was indistinguishable from that of natural sGH.Human growth hormone now can be produced by genetically engineered organisms and can be used as a therapeutic agent. Salmon growth hormone (sGH) can be synthesized by use of similar techniques, and the massive supply of sGH may be extremely important to fish culture. Growth hormone (GH), together with prolactin and chorionic somatomammotropin (placental lactogen), forms a set of proteins that are structurally related and have partially overlapping biological activities (1). Primary structure analysis of the peptides and of the genes suggests that these hormone genes evolved from a common ancestral origin (1-5). Therefore, these genes provide an excellent model system for studying structurefunction relationships, evolution, and regulation of expression. GH genes have been isolated from several mammalian species and characterized in detail (3,(6)(7)(8). To obtain information about the evolution and the mechanisms of organization of this set of genes, it is essential to compare the structures of these hormone genes isolated from many organisms at various evolutionary stages. No information, however, has been available about lower vertebrates such as fish.

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“…In reptiles, the purification of GHs from green sea turtle and snapping turtle pituitaries has been reported 5 .…”

Section: Introductionmentioning

confidence: 99%

Study on the Purification of Growth Hormone-Like Substance from Pituitaries of the SnakePlyas mucosa

Ng¹,

Lee²,

Chen³

et al. 1993

Preparative Biochemistry

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Extract from the snake (Ptyas mucosa) pituitaries was capable of inhibiting the binding of 125I-labelled bovine growth hormone to female rat liver membranes. The growth hormone-like substance was not adsorbed on Concanavalin A-Sepharose nor DEAE-cellulose, but could be purified by gel filtration on Sephadex G-50. It possessed a molecular weight of about 19,000 as judged by SDS-polyacrylamide gel electrophoresis. The iodinated snake growth hormone-like substance bound to membranes prepared from female rat and pregnant rabbit livers. The binding could be inhibited by unlabelled snake growth hormone-like substance as well as by bovine growth hormone.

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Purification and properties of teleost growth hormone

Cited by 84 publications

References 40 publications

Application of a sensitive radioimmunoassay for the measurement of growth hormone in gilthead sea bream (Sparus aurata) and other sparid fish

Application of a sensitive radioimmunoassay for the measurement of growth hormone in gilthead sea bream (Sparus aurata) and other sparid fish

Cloning and expression of cDNA for salmon growth hormone in Escherichia coli

Study on the Purification of Growth Hormone-Like Substance from Pituitaries of the SnakePlyas mucosa

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