scholarly journals Human pituitary growth hormone: a biologically active hendekakaihekaton peptide fragment corresponding to amino-acid residues 15-125 in the hormone molecule.

1975 ◽  
Vol 72 (10) ◽  
pp. 3878-3882 ◽  
Author(s):  
C. H. Li
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Biologically Active ◽  
Amino Acid Residues ◽  
Peptide Fragment ◽  
Human Pituitary ◽  
Pituitary Growth Hormone

Bovine growth hormone fragment (1–133) has in-vitro somatomedin-like activity

1983 ◽  
Vol 96 (2) ◽  
pp. 195-199 ◽  
Author(s):  
J. P. Liberti ◽  
L. A. Durham
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Costal Cartilage ◽  
Peptide Bond ◽  
Biologically Active ◽  
The Other ◽  
Bovine Growth Hormone ◽  
Amino Acid Residues ◽  
In Vitro Uptake

Thrombin digestion of bovine growth hormone (1–191) resulted in cleavage of the peptide bond between amino acid residues 133 and 134. Native growth hormone and purified peptides (1–133) and (134–191) were assayed for somatomedin-like activity. Peptide (1–133), ranging in concentration from 0·15–15 nmol/l, stimulated in-vitro uptake of [3H]thymidine by rat costal cartilage. None of the other peptides was biologically active.

scholarly journals The Amino Acid Composition of Human Pituitary Growth Hormone

1962 ◽  
Vol 45 (4) ◽  
pp. 176-178 ◽  
Author(s):  
Jonathan S. Dixon ◽  
Choh Hao Li
Keyword(s):  
Molecular Weight ◽  
Growth Hormone ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Acid Content ◽  
Empirical Formula ◽  
Amino Acid Content ◽  
Human Pituitary ◽  
Pituitary Growth Hormone

The amino acid content in human hypophyseal growth hormone has been determined by chromatography on resin columns. On the basis of 29,000 for the molecular weight, the empirical formula of the hormone was obtained: lys13his5arg14asp27 thr14ser23glu34pro12gly13ala12-(1/2 cys)6val12met4-ileu10leu31tyr10phe15try1(NH3)32.

Analogues of the cholecystokinin octapeptide modified in the central part of the molecule

1991 ◽  
Vol 56 (9) ◽  
pp. 1963-1970 ◽  
Author(s):  
Jan Hlaváček ◽  
Václav Čeřovský ◽  
Jana Pírková ◽  
Pavel Majer ◽  
Lenka Maletínská ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biological Activities ◽  
Point Of View ◽  
Biologically Active ◽  
Side Chain ◽  
Amino Acid Residues ◽  
Cholecystokinin Octapeptide ◽  
Biological Tests ◽  
Biological Potency ◽  
Biologically Active Conformation

In a series of analogues of the cholecystokinin octapeptide (CCK-8) the amino acid residues were gradually modified by substituting Gly by Pro in position 4, Trp by His in position 5, Met by Cle in position 6, or the Gly residue was inserted between Tyr and Met in positions 2 and 3 of the peptide chain, and in the case of the cholecystokinin heptapeptide (CCK-7) the Met residues were substituted by Nle or Aib. These peptides were investigated from the point of view of their biological potency in the peripheral and central region. From the results of the biological tests it follows that the modifications carried out in these analogues and in their Nα-Boc derivatives mean a suppression of the investigated biological activities by 2-3 orders of magnitude (at a maximum dose of the tested substance of 2 . 10-2 mg per animal).This means that a disturbance of the assumed biologically active conformation of CCK-8, connected with a considerable decrease of the biological potency of the molecule, takes place not only after introduction of the side chain into its centre (substitution of Gly4), but also after the modification of the side chains of the amino acids or by extension of the backbone in further positions around this central amino acid.

Synthesis of a Biologically Active Nonadecapeptide Corresponding to the First Nineteen Amino Acid Residues of Adrenocorticotropins1a

1961 ◽  
Vol 83 (21) ◽  
pp. 4449-4457 ◽  
Author(s):  
Choh Hao Li ◽  
Johannes Meienhofer ◽  
Eugen Schnabel ◽  
David Chung ◽  
Tung-Bin Lo ◽  
...  
Keyword(s):  
Amino Acid ◽  
Biologically Active ◽  
Amino Acid Residues
Sign in / Sign up

Export Citation Format

Share Document