Purification and Properties of Avian Growth Hormones

Farmer, Susan Walker; Papkoff, Harold; Hayáshida, T.

doi:10.1210/endo-95-6-1560

Cited by 60 publications

(15 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, somatotropins in the pituitary extracts of amphibian species (Rana catesbeiana and Necturus maculosus) showed reactions of only partial identity with somatotropin in extracts of pituitaries from the phylogenetically higher birds and reptiles. These results have been partially substantiated by later studies with monkey antiserum to rat somatotropin, in which purified somatotropins (9,10) were used instead of the crude pituitary extracts; these studies demonstrated reactions of identity between somatotropins of the turtle and several avian species.…”

mentioning

confidence: 91%

Pituitary growth hormones: further evidence for evolutionary conservatism based on immunochemical studies.

Hayáshida¹,

Farmer²,

Papkoff³

1975

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

View full text Add to dashboard Cite

Immunochemical relatedness of preparations of purified somatotropins (growth hormones) or somatotropins in pituitary extracts from various vertebrate species was investigated by applying an antiserum to a purified somatotropin from a submammalian species, the snapping turtle. With the exception of monkey somatotropin, all mammalian, reptilian, and avian preparations tested showed reactions of identity or near identity by immunodiffusion studies in agar gel. Radioimmunoassay employing labeled rat somatotropin as a tracer and for standards, revealed that these same pituitary preparations gave steep inhibition slopes that were parallel or nearly parallel to each other. Purified somatotropins or somatotropins in pituitary extracts of subreptilian species, including an amphibian and existing primitive fishes,showed partial yet substantial relatedness to mammalian (rat) or reptilian (turtle) somatotropins by both immunodiffusion and radioimmunoassay. Our evidence indicates that the immunochemical relatedness of somatotropins from various vertebrate species appears to be even closer than has been suggested previously, and that a high degree of conservation of structure occurs during evolution.Comparative studies conducted a few years ago with monkey antiserum to rat pituitary somatotropin indicated the existence of close immunochemical relatedness among somatotropins of numerous mammalian species (1-7), and further suggested that these hormones in crude extracts of pituitaries from submammalian species likewise showed significant, but decreasing immunochemical relatedness to mammalian somatotropins the greater the phylogenetic distance from the mammal (3). For example, somatotropins in extracts of pituitaries from several birds and reptiles gave qualitative reactions of partial identity when compared to mammalian somatotropins when tested in the agar gel diffusion test of Ouchterlony (8) The results of our most recent investigation are reported here in which the immunochemical relatedness of somatotropins from the various vertebrate species has been re-examined by using an antiserum to a purified somatotropin from a more primitive, phylogenetically lower species, the turtle, instead of an antiserum to a mammalian somatotropin (rat) that had been used in all of our earlier studies. We were curious to determine what differences, if any, in immunochemical relatedness of somatotropins might be observed by our taking such an approach. MATERIALS AND METHODSAntiserum was produced in rhesus monkeys by immunizing them with purified somatotropin prepared from frozen pituitary glands of the snapping turtle (Chelydra serpentina) (9, 10); an injection protocol similar to that previously described for the production of antisera to rat somatotropin in the same species was followed (1). Before use, the antiserum was absorbed with normal turtle serum and with purified ovine prolactin. The pituitary extracts to be tested were prepared from fresh frozen glands by homogenization in phosphatesaline buffer at pH 7.5 (1, 3). To inve...

show abstract

mentioning

confidence: 91%

Pituitary growth hormones: further evidence for evolutionary conservatism based on immunochemical studies.

Hayáshida¹,

Farmer²,

Papkoff³

1975

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

View full text Add to dashboard Cite

show abstract

“…Burke & Papkoff (1980) reported a molecular weight of 26 000. In general, the amino acid compositions of avian and mammalian gonadotrophins (Farmer, Papkoff & Licht, 1975;Godden & Scanes, 1975) and GH (Farmer et al, 1974) show remarkable similarity. The amino acid composition of our turkey prolactin, apart from the lack of methionine, was relatively similar to those reported for chicken prolactin and turkey prolactin, being rich in aspartic acid, glutamic acid and leucine.…”

Section: Discussionmentioning

confidence: 99%

“…The dose-response curve of each of these preparations was parallel to that of the ovine prolactin standard, indicating that the preparations were immunologically similar to ovine prolactin. In this assay the turkey growth hormone W130 DB, which was described by Farmer, Papkoff & Hayashida (1974), has <3-l% of the immunoactivity of ovine prolactin (Text-fig. 3).…”

Section: Introductionmentioning

confidence: 99%

Isolation and characterization of turkey prolactin

Cheng¹,

Etches²

1981

Reproduction

View full text Add to dashboard Cite

Summary. Prolactin from frozen turkey pituitary glands was purified by alkaline ethanol extraction of the pituitary residue after pre-extractions of the gonadotrophins and GH, followed by gel filtration on Sephadex G-100 and DEAE\p=m-\cellulosecolumn chromatography at different pH. A specific radioligand\p=m-\receptorassay for ovine prolactin was used to locate the activity in eluates after column chromatography and gel filtration. The potency of the highly purified turkey prolactin was characterized by a radioligand\p=m-\receptorassay to be 3\m=.\40 i.u./mg and by a heterologous radioimmunoassay to be 35 i.u./mg as compared to purified ovine prolactin as standard. The yield of turkey prolactin was 3 mg/100 g frozen pituitary glands. The purified turkey prolactin consisted of three protein bands upon polyacrylamide gel electrophoresis and the molecular weight was estimated to be 22 000 by SDS\p=m-\polyacryl-amide gel electrophoresis. Turkey prolactin was rich in aspartic acid, glutamic acid and leucine, but lacking in methionine.

show abstract

“…Chicken GH was purified according to the methods described by FARMER et al 5) and HARVEY and SCANES6) with a slight modification. Anterior pituitaries were collected from male and female broilers from a local killing plant (Ijichi Poultry Farm for 48hr with carrier ampholyte covering the pH range 3-10.…”

Section: Methodsmentioning

confidence: 99%

Purification and Properties of Chicken Growth Hormone

Tojo¹,

Fujii²,

Noiri³

et al. 1979

Nihon Chikusan Gakkaiho

View full text Add to dashboard Cite

Growth hormone (GH) was extracted and purified from the chicken anterior pituitaries and its properties were investigated. The procedure used in the present study consisted of alkaline extraction, ammonium sulfate precipitation, ion-exchange chromatography on Amberlite IRC-50, gel filtration on Sephadex G-75 and isoelectric focusing. The chicken GH obtained had a significant activity in increasing the width of the epiphyseal cartilage of tibia in the hypophysectomized chicken. The preparation was estimated to have a molecular weight of 25,800 by the sodium dodecyl sulfate polyacrylamide gel electrophoresis, a pI value of 7.93 by the isoelectric focusing and a cross-reactivity of about 2% with rat GH. Amino acid composition was very similar to those of chicken GH preparations described in the previous reports.Jap. J. Zootech. Sci., 50 (12): [863][864][865][866][867][868][869] 1979 The physiological role and the chemical properties of growth hormone (GH) have been extensively studied in many species of mammals. Although the existence of GH in chicken pituitary gland has been suggested by several investigators1-3), there were only a few reports4-6) concerning purification of GH and little is known about the role of GH. HARVEY and SCANES6) have purified chicken GH from the anterior pituitaries and have first developed the specific radioimmunoassay for the chicken GH. The authors also attempted to purify GH from chicken anterior pituitary glands and investigated its properties. Materials and MethodsChicken GH was purified according to the methods described by FARMER et al.5) and HARVEY and SCANES6) with a slight modification. Anterior pituitaries were collected from male and female broilers from a local killing plant (Ijichi Poultry Farm Jap.

show abstract

Purification and Properties of Avian Growth Hormones

Cited by 60 publications

References 0 publications

Pituitary growth hormones: further evidence for evolutionary conservatism based on immunochemical studies.

Pituitary growth hormones: further evidence for evolutionary conservatism based on immunochemical studies.

Isolation and characterization of turkey prolactin

Purification and Properties of Chicken Growth Hormone

Contact Info

Product

Resources

About