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

Increased Availability of Human Growth Hormone: A Challenge for Health Economics

1988 ◽  
Vol 4 (4) ◽  
pp. 629-633 ◽  
Author(s):  
Kerstin Albertsson-Wikland ◽  
Agne Larsson
Keyword(s):  
Decision Making ◽  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Gh Treatment ◽  
Pituitary Glands ◽  
Rapid Transition ◽  
Dna Technology ◽  
Constant Prices ◽  
Hybrid Dna

Human growth hormone (GH) has until recently been prepared commercially from pituitary glands collected at autopsy. Availability has been limited and cost high, so the indications for GH treatment have had to be “tight.” Owing to recent development in hybrid DNA technology, the availability of GH has increased dramatically. At the same time, the manufacturers have maintained constant prices, so that treatment costs continue to influence decision making about its use. This rapid transition has generated an interesting change of strategy, which is outlined in this review.

Localization of Fluorescent Antibodies to Human Growth Hormone in Human Anterior Pituitary Glands.

1960 ◽  
Vol 104 (2) ◽  
pp. 232-235 ◽  
Author(s):  
A. Leznoff ◽  
J. Fishman ◽  
L. Goodfriend ◽  
E. McGarry ◽  
J. Beck ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Anterior Pituitary ◽  
Human Growth ◽  
Pituitary Glands ◽  
Human Anterior Pituitary

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.

Cytoendocrinological findings in the pituitary glands of patients with psoriasis

1988 ◽  
Vol 119 (4) ◽  
pp. 501-505
Author(s):  
G. Weber ◽  
Ph. U. Heitz
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Pituitary Glands

Abstract. Twelve pituitary glands from patients suffering from psoriasis obtained at postmortem showed in all cases hyperplasia of human growth hormone-producing cells. These results support the postulated pathomechanism that psoriasis lesions may arise as a result of an increased production of human growth hormone.

scholarly journals Intra-molecular Conformational Stability in Human Growth Hormone

2020 ◽  
Vol 6 (2) ◽  
pp. 41-49
Author(s):  
R. P. Koirala ◽  
B. Thapa ◽  
S. P. Khanal ◽  
R. P. Adhikari ◽  
N. P. Adhikari
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Md Simulation ◽  
Conformational Stability ◽  
Human Growth ◽  
Anterior Lobe ◽  
Entire Structure ◽  
Drug Designing ◽  
Pituitary Glands ◽  
Binding Mechanisms

Human growth hormone (hGH) is synthesized, stored and secreted by somatotropic cells within the lateral wings of the anterior lobe of pituitary glands; and is transported to other organs of human body. Study of intra-molecular structure and its binding mechanisms within the molecule gives more insight of structural stability of the molecule and is also essential in drug designing. In this article, we have investigated the various bonded and non-bonded interactions that contribute for the conformation of entire structure of the hGH molecule using molecular dynamics (MD) simulation. The MD outcomes show that the molecule is hydrophobic in nature. In its conformation, several types of interactions exist, such as disulphide bridges (bonded) and nonbonded: hydrogen bond, hydrophobic, aromatic-aromatic, ionic, aromatic-sulphur, cation-pi.

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?

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.

LARGE-SCALE PREPARATION OF HIGHLY PURIFIED PYROGEN-FREE HUMAN GROWTH HORMONE FOR CLINICAL USE

1979 ◽  
Vol 82 (1) ◽  
pp. 77-86 ◽  
Author(s):  
R. LUMLEY JONES ◽  
G. BENKER ◽  
P. R. SALACINSKI ◽  
T. J. LLOYD ◽  
P. J. LOWRY
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Large Scale ◽  
Gel Filtration ◽  
Human Growth ◽  
Exchange Chromatography ◽  
Large Scale Preparation ◽  
Alkaline Conditions ◽  
Pituitary Glands ◽  
Scale Preparation

SUMMARY A method is described for the large-scale isolation of highly purified human growth hormone for therapeutic use. The hormone was extracted from frozen pituitary glands under mildly alkaline conditions. Purification was effected by gel filtration and ion-exchange chromatography. The final product was pyrogen-free and had a potency of 2·5 i.u./mg measured by bioassay against the current international standard. The yield of growth hormone/gland was approximately 5 mg.

Sign in / Sign up

Export Citation Format

Share Document