Molecular Formula | C990H1529N263O299S7 |
Molar Mass | 22124.12 |
Specific Rotation(α) | 25 -38.7° (0.1M acetic acid) |
Appearance | lyophilized powder |
Storage Condition | 2-8°C |
Use | Summary The human growth hormone (GH) is a single-chain, non-glycated, hydrophilic globulin of 191 amino acids with a molecular weight of 21700Da and an isoelectric point pI of 4.9. At positions 53 and 165 and 182 and 189 cysteine residues are linked by disulfide bonds; Approximately 75% of the growth hormone secreted by the eosinophils of the anterior pituitary gland is secreted in the form of this molecular structure, another 5-10% is secreted in the form of molecular weight 20kDa. |
WGK Germany | 3 |
RTECS | TO7385000 |
HS Code | 2937110000 |
Toxicity | LD50 oral in rat: 160iu/kg |
Overview | human Growth hormone (GH) is a single-chain, non-glycosylated, A hydrophilic globulin consisting of 191 amino acids with a molecular weight of 21700Da and an isoelectric point pI of 4.9. At positions 53 and 165 and 182 and 189 cysteine residues are linked by disulfide bonds; Approximately 75% of the growth hormone secreted by the eosinophils of the anterior pituitary gland is secreted in the form of this molecular structure, another 5-10% is secreted in the form of molecular weight 20kDa. |
secretion | spontaneous secretion of hGH in a paroxysmal form, it usually occurs in the first slow wave sleep period (SWS) after physiological sleep. Rest during the day may promote the release of hGH, feeding, fasting, exercise and stress can affect the secretion of hGH, but does not change its basic rhythm; Adolescent hGH secretion amplitude, frequency, the total amount of diurnal secretion is large, while the elderly are the opposite. |
properties | human growth hormone pre-hormone is composed of growth hormone naturally present in bacteria, linked to a signal peptide. The prohormone divides in the inner wall of the cell of the bacterium, releasing the same final product as the natural growth hormone into the intramural membrane space, and then only destroying the outer wall of the cell to collect, while the inner wall of the cell remains intact, in order to ensure that there is little bacterial protein contamination of the final product. |
Li Yuanxin , Li Yousheng , Ren Jianan Li-Ning , Li Jianxiong
Abstract:
Objective: to study the effect of recombinant human growth hormone on protein metabolism in patients with chronic abdominal infection. Methods: Twenty patients with chronic abdominal infection were randomly divided into GH group (TPN GH) and control group (TPN). Infection score, serum growth hormone (GH), serum insulin-like growth factor -1(IGF-1), serum insulin-like growth factor binding protein -3(IGFBP-3); Serum albumin, prealbumin, transferrin, fibronectin, C- reactive protein; Determination of daily nitrogen balance and 24 h urine creatinine. Results: at the end of the study, GH,IGF-1,IGFBP-3 in the GH group were significantly higher than those in the control group and before the study, C- reactive protein decreased; Nitrogen balance improved, the cumulative nitrogen balance was significantly higher than the control group, while 24 h urinary creatinine decreased. Conclusion: recombinant human growth hormone can promote protein metabolism in patients with chronic abdominal infection, and IGF-1 plays an important role in it.stowed
Key words:
infection metabolism Growth hormone Serum Albumin
DOI:
10.3969/j.issn.1007-810X.2001.01.002
cited:
year:
2001
Abstract:
objective: to observe the effect of recombinant human growth hormone (rhGH) on the proliferation of human umbilical vein endothelial cells (ECV) co-cultured with hepatoma cell lines expressing different growth hormone receptors (GHR). Methods: The GHR positive and negative cell lines were screened by immunocytochemistry and co-cultured with ECV. The intervention was performed with different concentrations of rhGH(50 and 250ng/mL, blank control). The proportion of cell cycle was detected by flow cytometry. The concentration of vascular endothelial growth factor (VEGF) secreted by hepatoma cells was determined by ELISA, and the cell growth curve was drawn. Results: Bel-7402(GHR positive) increased the level of VEGF secretion after rhGH intervention, and the growth of ECV co-cultured with rhGH was accelerated, and the proportion of S phase cells was significantly increased in a concentration-dependent manner (P 〈 0.05).. While SMMC-7721(GHR negative) could promote ECV proliferation, but was not affected by rhGH, and the secretion of VEGF did not change (P 〉 0.05). Conclusion: rhGH can induce GHR() hepatoma cells to secrete VEGF and indirectly promote the proliferation of vascular endothelial cells.
stowed
Key words:
Growth hormone growth hormone receptor angiogenesis co-culture
DOI:
CNKI:SUN:CWCN.0.2008-04-003
cited:
year:
2008
Abstract:
growth hormone (GH) has been used in clinical burn for half a century. It was isolated from the bovine pituitary gland and named by Li zuohao, a Chinese Canadian scholar in the 40's of the 20th century. In 1956, Li Zuo made great efforts to purify human growth hormone (hGH), thus attracting many scholars, such as endocrinology, metabolism, nutrition and pathophysiology and other experts to conduct in-depth research, and has basically clarified its biochemical characteristics and physiological effects, growth hormone and other hormones and growth hormone secretion regulation mechanism, among them, the experimental studies on the growth promoting effect of GH in rats, dogs and monkeys are still authoritative literatures, and GH species specificity has been known, and has been included in the hormone replacement therapy of GH endocrine dysfunction [1].
Key words:
Growth hormone GH burn human growth hormone Nutrition immunology
DOI:
CNKI:SUN:ZHSA.0.2001-04-000
cited:
year:
2001