IMMUNOCHEMICAL STUDIES OF HUMAN GROWTH HORMONE, OVINE PROLACTIN, BOVINE GROWTH HORMONE AND A TRYPTIC DIGEST OF BOVINE GROWTH HORMONE

1969 ◽  
Vol 44 (4) ◽  
pp. 517-NP ◽  
Author(s):  
KALYAN SUNDARAM ◽  
M. SONENBERG

SUMMARY Agar gel double diffusion and immunoelectrophoresis of human growth hormone (HGH), ovine prolactin, bovine growth hormone (BGH) and a tryptic digest of BGH (TBGH) were performed. Antisera to BGH, TBGH, HGH and ovine prolactin were used for the tests. Both BGH and TBGH were found to contain material that precipitated with antiserum to ovine prolactin. Immunological analysis of various fractions of BGH and TBGH separated by chromatography on DEAE-cellulose showed that BGH and TBGH were eluted before prolactin. No differences between BGH and TBGH in their immunological reactions were found. HGH did not cross-react with BGH, TBGH or ovine prolactin.

1969 ◽  
Vol 60 (1) ◽  
pp. 101-111 ◽  
Author(s):  
W. Rohde ◽  
G. Dörner

ABSTRACT The specific antigenic patterns of human growth hormone in various human pituitary extracts were determined by analysis in gel filtration, in starch gel and agar gel immunoelectrophoresis. The analysis of pituitary extracts by gel filtration on Sephadex G-200 indicates that HGH complexes with different molecular weights were present in all tested pituitary extracts. The rate of formation of high molecular HGH was dependent on the extraction procedure used. Altogether seven immunologically active components of HGH were detected by analysis of crude pituitary extracts in starch gel immunoelectrophoresis. The number and the rate of formed HGH components were dependent on the solvent used for the extraction of pituitary homogenates and on the sequence of extraction procedures. The electrophoretical patterns obtained were reproducible. The electrophoretical behaviour of HGH of various pituitary extracts in agar gel also suggested the presence of multiple components. Three different positions were observed between the α1- and β1-globulins. The analysis of pituitary extracts in the two dimensional double diffusion technique in agar gel using an absorbed anti-HGH-serum gave evidence of the antigenic homogeneity of HGH in the different preparations. It is concluded that the electrophoretic heterogeneity of pituitary growth hormone preparations is already determined by the first step of the extraction.


1969 ◽  
Vol 43 (4) ◽  
pp. 651-662 ◽  
Author(s):  
A. T. COWIE ◽  
P. E. HARTMANN ◽  
A. TURVEY

SUMMARY Twenty-one rabbits were hypophysectomized during the second week of lactation. Hypophysectomy inhibited milk secretion within 3–7 days. Restoration of the milk yield to pre-operative levels was obtained when daily injections of either sheep prolactin (50 or 100 i.u.) or human growth hormone (HGH) (2·5 or 5 mg.) were administered; partial recovery of the milk yield was obtained with 25 i.u. sheep prolactin/day or 1·25 mg. HGH/day. Neither bovine growth hormone (BGH), adrenocorticotrophin (ACTH) nor cortisol acetate had any significant restorative effects on milk secretion or synergistic effects when combined with sheep prolactin or HGH. The probable development of immune responses to sheep prolactin and HGH was observed. After hypophysectomy, changes in milk composition were found which were similar in trend to the more gradual normal changes observed in late lactation. Sheep prolactin and HGH restored the composition of the milk as well as the yields to normal levels, and both hormones caused rapid increases in lactose yields. The pigeon crop-stimulating potency of the HGH preparation was low (equivalent to 3·7 i.u. sheep prolactin/mg.), yet its lactogenic and galactopoietic potencies were high thus emphasizing the unreliability of assessing the mammotrophic potencies of HGH preparations in birds.


Endocrinology ◽  
1986 ◽  
Vol 118 (2) ◽  
pp. 720-726 ◽  
Author(s):  
ARIEH GERTLER ◽  
AVI SHAMAY ◽  
NAVA COHEN ◽  
AVI ASHKENAZI ◽  
HENRY G. FRIESEN ◽  
...  

1964 ◽  
Vol 46 (3) ◽  
pp. 465-472 ◽  
Author(s):  
Zvi Laron ◽  
Ariana Yed-Lekach ◽  
Sara Assa ◽  
Avivah Kowadlo-Silbergeld

ABSTRACT Human, bovine and sheep (ovine) growth hormone (HGH, BGH and SGH) were heated in solution at temperatures between 60 and 100 °C. The electrophoretic mobility and immunological properties, such as precipitation reactions in agar gel and haemagglutination with antiserum to untreated hormone, were studied at different degrees of heating. It was found that heat progressively reduced the immunological properties of the growth hormone; however, human growth hormone was more resistant to heat treatment than the bovine and sheep growth hormone. HGH retained precipitation properties when heated at 100° C up to 30 minutes, and reacted in the haemagglutination test when heated at 100° C for less than 60 minutes. BGH and SGH clotted at 100° C. The precipitation reaction with antiserum to BGH disappeared when BGH or SGH was heated at 70° C for more than 10 minutes. Only a weak haemagglutination reaction was retained when BGH or SGH was heated at 80° C for 15 minutes.


1991 ◽  
Vol 45 (1) ◽  
pp. 178-187 ◽  
Author(s):  
Erick M. Naar ◽  
Andrzej Bartke ◽  
Subeer S. Majumdar ◽  
Frances C. Buonomo ◽  
Jeung S. Yun ◽  
...  

1970 ◽  
Vol 63 (4) ◽  
pp. 736-746 ◽  
Author(s):  
David B. Grant ◽  
Selna L. Kaplan ◽  
Melvin M. Grumbach

ABSTRACT The properties of a monkey placental protein (monkey chorionic somatomammotrophin; MCS) which reacts with antisera directed against human growth hormone (HGH) and human chorionic somatomammotrophin (HCS) have been studied. Following application of monkey placental extracts to Sephadex G-100 and elution with 0.1 m NH4HCO3, two peaks of MCS, with molecular weights of approximately 25 000 and 50 000 were obtained. The electrophoretic mobility of MCS in acrylamide at pH 8.2–8.4 was similar to but less anodal than that of HGH or HCS. The results of immunoelectrophoretic and Ouchterlony double-diffusion studies indicated that MCS is physicochemically and immunochemically distinguishable from HGH and HCS. When tested in a radioimmunoassay for HGH, MCS gave dilution curves intermediate between those for HGH and HCS. In contrast, MCS and HGH gave similar curves in a radioimmunoassay for HCS. MCS, HCS and HGH had very similar effects on the reactions between 131I-HGH and anti-HCS or 131I-HCS and anti-HGH serum. Radioimmunoassay systems for HCS were unsuitable for estimating MCS; however, the above mentioned hybrid assay systems provide a means for approximate quantitation of MCS.


1970 ◽  
Vol 48 (3) ◽  
pp. 433-NP ◽  
Author(s):  
P. E. HARTMANN ◽  
A. T. COWIE ◽  
ZENA D. HOSKING

SUMMARY Five groups of five lactating rabbits each were used. Milk yield was recorded from the 8th day of lactation onwards and on the 10th day of lactation the rabbits received the following treatments: Group S, sham-operation with saline (1 ml/12 h); Group P, hypophysectomy with sheep prolactin (1 mg/12 h); Group H, hypophysectomy with human growth hormone (1 mg/12 h); Group B, hypophysectomy with bovine growth hormone (1 mg/12 h) and Group C, hypophysectomy with saline (1 ml/12 h). The injections of saline or hormones were continued for 5 days and at the end of this period a blood sample was taken, the animals were killed and their mammary glands removed for histological examination and assay of the following enzymes: 6-phosphogluconate dehydrogenase (EC 1.1.1.44), phosphofructokinase (EC 2.7.1.11), phosphoglucomutase (EC 2.7.5.1), UDP-glucose pyrophosphorylase (EC 2.7.7.9), acetyl-CoA carboxylase (EC 6.4.1.2), acetyl-CoA synthetase (EC 6.2.1.1) and ATP-citrate lyase (EC 4.1.3.8). On the 5th day after surgery the concentrations of blood l-lactate and pyruvate and plasma free fatty acids and protein were similar in all groups, whereas plasma glucose was higher in groups S, B and H than in groups P and C. Although the weights of pituitary target organs (adrenals, thyroid and ovaries) were similar in all groups, the weights (g/kg body weight) of mammary tissue varied markedly, group S being the heaviest and group C the lightest. Milk yields, 5 days after surgery, for groups P and H were about 50% that for S, whereas those for B and C were 15 and 4% respectively. Where possible the enzyme activity was expressed as a ratio of the rate of synthesis of the end product of the pathway in which the enzyme occurred. With the exception of acetyl-CoA carboxylase which may have had a rate-limiting role in the synthesis of milk fat, enzymic activity in vitro was in excess of that required in vivo for the synthesis of either milk fat or lactose. It appeared that the rate of milk synthesis depended upon the degree of maintenance of the secretory epithelial cells within the mammary gland rather than a block in the synthetic pathways within these cells.


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