Effect of N-methylation of the peptide bond in the C-terminal part of the B-chain of human insulin on biological activity

2001 ◽  
Author(s):  
Lenka Klasová ◽  
Štefan Zorad ◽  
Jiří Velek ◽  
Jan Ježek ◽  
Václav Kašička ◽  
...  
Keyword(s):  
Biological Activity ◽  
Human Insulin ◽  
Peptide Bond ◽  
Terminal Part

scholarly journals Biological activity of synthetic human insulin

Diabetologia ◽  
1977 ◽  
Vol 13 (4) ◽  
pp. 293-295 ◽  
Author(s):  
F. M�rki ◽  
W. Albrecht
Keyword(s):  
Biological Activity ◽  
Human Insulin

Synthesis and biological activity of five d-Cys analogs of human insulin

1979 ◽  
Vol 8 (4) ◽  
pp. 443-450 ◽  
Author(s):  
K. Eisler ◽  
B. Kamber ◽  
B. Riniker ◽  
W. Rittel ◽  
P. Sieber ◽  
...  
Keyword(s):  
Biological Activity ◽  
Human Insulin

scholarly journals Immunochemical studies on human calcitonin M leading to information on the shape of the molecule

1972 ◽  
Vol 127 (1) ◽  
pp. 199-206 ◽  
Author(s):  
P. G. H. Byfield ◽  
M. B. Clark ◽  
K. Turner ◽  
G. V. Foster ◽  
I. MacIntyre
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Sites ◽  
Peptide Bond ◽  
Peptide Chain ◽  
Human Calcitonin ◽  
Covalent Interaction ◽  
Different Parts

1. Two antisera were obtained from a single rabbit. Both are highly specific for human calcitonin M but react with different parts of the amino acid sequence. 2. The different sequences that react with the antibodies of the two antisera were located. The first antiserum reacts at two sites in the molecule, one in the sequence residues 11–18, probably with residue 17 as the immunodominant group, and another on either side of the 28–29 peptide bond. The second antiserum, harvested 9 months later, reacts principally at one site bridging the 28–29 peptide bond. 3. A consideration of the properties of the hormone's binding sites and of data relating biological activity to structure enables some conclusions to be drawn with regard to the shape of the molecule. It appears that the peptide chain is folded to bring N- and C-termini closer together and that there is non-covalent interaction between regions in the chain near both termini. One of these is located near residue 8.

Synthesis and Biological Activity of Two Disulphide Bond Isomers of Human Insulin: [A7-A11 ,A6-B7-Cystine]- and [A6-A7,A11-B7-Cystine]insulin (Human)

1978 ◽  
Vol 359 (1) ◽  
Author(s):  
Peter Sieber ◽  
Karel Eisler ◽  
Bruno Kamber ◽  
Bernhard Riniker ◽  
Werner Rittel ◽  
...  
Keyword(s):  
Biological Activity ◽  
Human Insulin ◽  
Disulphide Bond ◽  
Bond Isomers

scholarly journals A new non-covalent complex of semisynthetically modified tryptic fragments of cytochrome c

1986 ◽  
Vol 239 (2) ◽  
pp. 333-337 ◽  
Author(s):  
A E Proudfoot ◽  
C J Wallace ◽  
D E Harris ◽  
R E Offord
Keyword(s):  
Biological Activity ◽  
Cytochrome C ◽  
Redox Potential ◽  
Peptide Bond ◽  
Succinate Oxidation ◽  
Covalent Complex ◽  
Horse Cytochrome

We have prepared a semisynthetic analogue of fully acetimidylated horse cytochrome c, a complex in which the peptide bond between residues glycine-37 and arginine-38 is lacking. In contrast with the complex that we have previously described [Harris & Offord (1977) Biochem. J. 161, 12-25], in which the break in continuity is between residues arginine-38 and lysine-39, the new analogue has a nearly normal redox potential, and can more fully restore succinate oxidation to mitochondria depleted of cytochrome c. Studies of this and other analogues lead us to propose an explanation for the low biological activity of complex (1-38)-(39-104) and a role for the invariance of arginine-38.

Possible involvement of the A20-A21 peptide bond in the expression of the biological activity of insulin. 1. [21-Desasparagine,20-cysteinamide-A]insulin and [21-desasparagine,20-cysteine isopropylamide-A]insulin

Biochemistry ◽  
1987 ◽  
Vol 26 (22) ◽  
pp. 6966-6971 ◽  
Author(s):  
Ying Chi Chu ◽  
Run Ying Wang ◽  
G. Thompson Burke ◽  
Jacob D. Chanley ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Peptide Bond

Possible involvement of the A20-A21 peptide bond in the expression of the biological activity of insulin. 2. [21-Asparagine diethylamide-A]insulin

Biochemistry ◽  
1987 ◽  
Vol 26 (22) ◽  
pp. 6972-6975 ◽  
Author(s):  
Ying Chi Chu ◽  
G. Thompson Burke ◽  
Jacob D. Chanley ◽  
Panayotis Katsoyannis
Keyword(s):  
Biological Activity ◽  
Peptide Bond

Equivalent In Vivo Biological Activity of Insulin Analogues and Human Insulin Despite Different In Vitro Potencies

Diabetes ◽  
1990 ◽  
Vol 39 (9) ◽  
pp. 1033-1039 ◽  
Author(s):  
U. Ribel ◽  
P. Hougaard ◽  
K. Drejer ◽  
A. R. Sorensen
Keyword(s):  
Biological Activity ◽  
Human Insulin ◽  
Insulin Analogues

Analogs of arginine vasopressin modified in theN-terminal part of the molecule with a conformationally constrainedcis-peptide bond motif

2007 ◽  
Vol 13 (2) ◽  
pp. 128-132 ◽  
Author(s):  
Dariusz Sobolewski ◽  
Adam Prahl ◽  
Izabela Derdowska ◽  
Jiřina Slaninová ◽  
Krzysztof Kaczmarek ◽  
...  
Keyword(s):  
Arginine Vasopressin ◽  
Peptide Bond ◽  
Terminal Part
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