The relationship of human growth hormone and plasma tyrosine during sleep.

1971 ◽  
Author(s):  
Leonard M. Zir ◽  
Donald C. Parker ◽  
Richard A. Smith ◽  
Lawrence G. Rossman
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Plasma Tyrosine ◽  
Relationship Of ◽  
The Relationship

The Relationship of Human Growth Hormone and Plasma Tyrosine During Sleep

1972 ◽  
Vol 34 (1) ◽  
pp. 1-6 ◽  
Author(s):  
LEONARD M. ZIR ◽  
DONAL C. PARKER ◽  
RICHARD A. SMITH ◽  
LAWRENCE G. ROSSMAN
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Human Growth ◽  
Plasma Tyrosine ◽  
Relationship Of ◽  
The Relationship

Fractionation Studies on Plasma of Normals and Patients with Laron Dwarfism and Hypopituitary Gigantism

1973 ◽  
Vol 51 (11) ◽  
pp. 845-852 ◽  
Author(s):  
R. M. Bala ◽  
J. C. Beck
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Size Range ◽  
Human Growth ◽  
Molecular Size ◽  
Relative Increase ◽  
Normal Serum ◽  
Main Peak ◽  
Relationship Of ◽  
The Relationship

The molecular size of immunoreactive human growth hormone (IR-HGH) in serum and the relationship of IR-HGH to sulfation factor (SF) require further investigation. Sera obtained from normal volunteers, patients with Laron-type dwarfism, and hypopituitary patients with gigantism were fractionated on large columns of Sephadex. The IR-HGH in normal serum was found in a molecular size range similar to extracted pituitary HGH (epHGH), as well as in a larger and a smaller molecular size. Laron dwarf plasma had a similar molecular size IR-HGH distribution when compared with normal serum. Sera from hypopituitary patients with gigantism showed an increased relative amount of small IR-HGH compared with normal serum. SF activity was recovered in normal serum but not in other sera fractions. SF activity appeared mainly in the molecular size range less than 17 000 and another peak was noted in the molecular size area greater than 55 000.This study further supports the existence of IR-HGH in a large and a small molecular size in normal serum. IR-HGH in Laron dwarf serum appears similar in molecular size to normal serum IR-HGH. The relative increase in small IR-HGH in hypopituitary patients with gigantism requires further investigation. SF activity appears in a molecular size different from epHGH in normal serum, the main peak being in a smaller molecular size area, with a lesser peak in a larger size area.

Biological activities of human growth hormone and its derivatives estimated by measuring DNA synthesis in Nb2 node rat lymphoma cells

1987 ◽  
Vol 114 (2) ◽  
pp. 283-291 ◽  
Author(s):  
Naoya Emoto ◽  
Toshio Tsushima ◽  
Kazuo Shizume ◽  
Toshiaki Tanaka ◽  
Motoyasu Saji ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Dna Synthesis ◽  
Human Growth Hormone ◽  
Receptor Binding ◽  
Human Growth ◽  
Suitable Model ◽  
Dependent Manner ◽  
Nb2 Cells ◽  
The Relationship ◽  
Stimulation Of

Abstract. Nb2 cell is a rat lymphoma cell line that responds to lactogens such as prolactin and human growth hormone (hGH) with an increased rate of proliferation. We explored the relationship between the biochemical events induced by hGH and its derivatives and their receptor binding activities. hGH stimulated RNA, DNA and protein synthesis of Nb2 cells as a function of time. Stimulation of RNA and protein was maximal at 2–3 h and 12 h, respectively, after the addition of hGH. DNA synthesis, measured by the rate of [3H]thymidine incorporation, reached a maximum after 18-h incubation with hGH. Stimulation of DNA synthesis was elicited by hGH in a dose-dependent manner between 0.45 and 45 pmol/l. The activity of the 20 K hGH variant in stimulating DNA synthesis was approx 30% of that of hGH. In contrast, S1-hGH, which lacks a sequence of ten amino acids (140–149) of hGH, showed a 3.2-fold greater activity than hGH. F1 (aminoterminal sequence 1–134 of hGH) was only 0.06% as active as hGH, and the activity of F2 (C-terminal 42 amino acid residue of hGH) was less than 0.01%. Both fragment 1–15 and 32–46 were without effect. The relative potencies of these hGH derivatives in stimulating DNA synthesis were similar to their relative abilities to inhibit [125I]hGH binding to lactogenic receptors on Nb2 cell. Nb2 cells provide a suitable model to study the relationship between receptor binding and the biochemical events induced by lactogens.

LIPOLYTIC ACTIVITY OF ENZYME DIGESTED HUMAN GROWTH HORMONE

1965 ◽  
Vol 49 (3_Suppl) ◽  
pp. S143
Author(s):  
Zvi Laron ◽  
Avivah Kowadlo-Silbergeld
Keyword(s):  
Growth Hormone ◽  
Human Growth Hormone ◽  
Lipolytic Activity ◽  
Human Growth

The minimal amino acid sequence of the insulin-potentiating fragments of human growth hormone: its mechanism of action

Diabetes ◽  
1980 ◽  
Vol 29 (10) ◽  
pp. 782-787 ◽  
Author(s):  
F. M. Ng ◽  
J. Bornstein ◽  
C. E. Pullin ◽  
J. O. Bromley ◽  
S. L. Macaulay
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Growth Hormone ◽  
Mechanism Of Action ◽  
Human Growth
Sign in / Sign up

Export Citation Format

Share Document