RADIOIMMUNOASSAY STUDIES WITH HUMAN GROWTH HORMONE AND A PITUITARY LIPID MOBILIZING FACTOR

1968 ◽  
Vol 58 (2) ◽  
pp. 318-338 ◽  
Author(s):  
N. Norman ◽  
Aa. R. Turter
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Antibody Formation ◽  
Human Growth ◽  
Structural Features ◽  
The Other ◽  
Human Pituitary ◽  
Pituitary Glands ◽  
Growth Promoting ◽  
The One

ABSTRACT A description is given of a radioimmunoassay procedure for human growth hormone (HGH). Particular emphasis is placed on problems encountered with aggregation and unspecific serum protein binding of the 125I radioiodinated HGH. Immunization of rabbits and guinea pigs with a highly purified lipid mobilizing factor (LMF) from human pituitary glands was attempted. This did not result in antibody formation towards LMF, but gave high titers against HGH. The observation thus suggests that LMF may have structural features in common with the HGH molecule. The antibody towards HGH may, however, also have been produced by a minimal contamination with HGH in the LMF. It was shown that detectable antibody formation towards HGH could be produced in rabbits with as little as 5 μg HGH. During the study of two highly purified HGH preparations – the one containing only growth promoting or somatotrophic activity, the other had adipokinetic activity as well - it was shown that the employed radioimmunoassay is specifically directed against the growth promoting part of HGH. Changes in the serum concentration of a possible physiologically acting LMF could therefore not be recorded, neither by a direct assay nor indirectly. On the other hand, the specificity of the HGH assay towards the »somatotrophin proper« assures that it is indeed this hormone that varies in concentration in response to insulin hypoglycaemia, exercise and postprandially. The stress of acute cardiac infarction did not increase growth hormone in the blood.

IMMUNOCHEMICAL STUDIES OF HUMAN PITUITARY GROWTH HORMONE

1962 ◽  
Vol 40 (2) ◽  
pp. 311-320 ◽  
Author(s):  
Zvi Laron ◽  
Sara Assa
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Haemagglutination Inhibition ◽  
Rabbit Antiserum ◽  
Human Growth ◽  
Human Albumin ◽  
Agar Gel ◽  
Human Pituitary ◽  
Pituitary Glands ◽  
Fraction I

ABSTRACT Human growth hormone (HGH) prepared from human pituitary glands by the method of Raben (1959) showed two components on agar gel electrophoresis. Fraction I corresponded to a slow alpha-globulin, and fraction II had a mobility between alpha and beta-globulin. On agar gel immunoelectrophoresis using HGH and rabbit antiserum to HGH, these two components showed immunological identity. By using agar gel immunoelectrophoresis and the haemagglutination technique HGH preparations of both Raben and Li type were shown to be contaminated with human albumin. Antiserum to human growth hormone containing also antibodies against human albumin was purified by adsorption with human albumin. It is postulated that part of the difficulties encountered in the use of the haemagglutination-inhibition technique to determine growth hormone concentration in serum, is due to impurities in the human growth hormone preparations and antisera to these preparations in use.

Using human growth hormone (somatropin)

1989 ◽  
Vol 27 (25) ◽  
pp. 97-98
Keyword(s):  
Growth Hormone ◽  
Young Adults ◽  
Short Stature ◽  
Human Growth Hormone ◽  
Gh Deficiency ◽  
Human Growth ◽  
Turner’S Syndrome ◽  
Human Pituitary ◽  
Pituitary Glands ◽  
Jakob Disease

Short stature was first treated in 1958 with growth hormone (GH) made from human pituitary glands.1 In 1985 biosynthetic GH was introduced after several young adults treated with GH in childhood had died from Creutzfeldt-Jakob disease.2 The first biosynthetic GH somatrem (Somatonorm - KabiVitrum) contains an additional methionyl residue and is licensed for treating short stature of Turner’s syndrome as well as GH deficiency. A preparation identical to human GH is now available (somatropin (rbe); Genotropin - KabiVitrum). Who should have it?

scholarly journals Adrenarche and pubarche in girls with turner syndrome during growth-promoting therapy with human growth hormone

2019 ◽  
Vol 19 (1) ◽  
Author(s):  
Helmuth G. Dörr ◽  
Theresa Penger ◽  
Michaela Marx ◽  
Manfred Rauh ◽  
Patricia G. Oppelt ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Turner Syndrome ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Growth Promoting

Human growth hormone peptide 1?43: Isolation from pituitary glands

1983 ◽  
Vol 2 (6) ◽  
pp. 425-436 ◽  
Author(s):  
Rama N. P. Singh ◽  
Boyd K. Seavey ◽  
Loraine J. Lewis ◽  
Urban J. Lewis
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Pituitary Glands

Isolated human growth hormone deficiency due to the hGH-I gene deletion with (type IA) and without (the Israeli-type) hGH antibody formation during hGH therapy

1990 ◽  
Vol 122 (2) ◽  
pp. 267-271 ◽  
Author(s):  
Yoshikazu Nishi ◽  
Hiroyuki Masuda ◽  
Shinichiro Nishimura ◽  
Mikio Kihara ◽  
Seizo Suwa ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Hormone Deficiency ◽  
Human Growth Hormone ◽  
Antibody Formation ◽  
Gene Deletion ◽  
Human Growth ◽  
Japanese Patients ◽  
Hormone Deficiency ◽  
Growth Responses ◽  
I Gene

Abstract Three Japanese patients with isolated growth hormone deficiency from two different families were shown to be homozygous for deletion of the structural gene for human growth hormone (hGH-I gene). These three patients had the same restriction fragment length polymorphism haplotypes. In patient No. 1, the growth rate initially responded well to pituitary human growth hormone, but growth rapidly ceased concomitantly with the development of high levels of anti-hGH antibodies. He again responded well to recombinant methionyl hGH and recombinant hGH without the methionine residue, even though having high hGH antibodies. Two siblings (Patients No. 2 and 3) showed a rather good response to pituitary hGH treatment without hGH antibodies ever being detected (the Israeli-type). hGH-I gene deletions may not necessarily result in hGH antibody formation. Heterogeneity has been observed in isolated hGH deficiency due to hGH-I gene deletion. hGH-I gene analysis should not be limited to patients with hGH antibody formation and subnormal growth responses to hGH therapy.

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