Possible involvement of the A20-A21 peptide bond in the expression of the biological activity of insulin. 3. [21-Desasparagine,20-cysteine ethylamide-A]insulin and [21-desasparagine,20-cysteine 2,2,2-trifluoroethylamide-A]insulin

Biochemistry ◽  
1987 ◽  
Vol 26 (22) ◽  
pp. 6975-6979 ◽  
Author(s):  
Ying Chi Chu ◽  
Run Ying Wang ◽  
G. Thompson Burke ◽  
Jacob D. Chanley ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Peptide Bond

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.

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

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

Role of Peptide Bond in the Realization of Biological Activity of Short Peptides

2015 ◽  
Vol 158 (4) ◽  
pp. 551-554
Author(s):  
V. Kh. Khavinson ◽  
S. I. Tarnovskaya ◽  
N. S. Lin’kova ◽  
N. A. Chervyakova ◽  
T. E. Nichik ◽  
...  
Keyword(s):  
Biological Activity ◽  
Peptide Bond ◽  
Short Peptides

Double bond isosteres of the peptide bond: Synthesis and biological activity of cholecystokinin (CCK) C-terminal hexapeptide analogs

1993 ◽  
Vol 1 (3) ◽  
pp. 161-171 ◽  
Author(s):  
Youe-Kong Shue ◽  
Michael D. Tufano ◽  
George M. Carrera ◽  
Hana Kopecka ◽  
Sharon L. Kuyper ◽  
...  
Keyword(s):  
Biological Activity ◽  
Double Bond ◽  
Peptide Bond

Backbone-modified oligopeptidic bioregulators. The synthesis and configuration of thioamide, amidoxime, cyanoamidine, and amidrazone analogs of the chemotactic peptide N-formyl-methionyl-leucyl-phenylalanine (f-Met-Leu-Phe-OR)

1985 ◽  
Vol 63 (11) ◽  
pp. 3089-3101 ◽  
Author(s):  
Gilles Sauvé ◽  
Vanga S. Rao ◽  
Gilles Lajoie ◽  
Bernard Belleau
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Biological Activity ◽  
Magnetic Resonance ◽  
Peptide Bond ◽  
Chemotactic Peptide ◽  
Reaction Conditions ◽  
Nuclear Magnetic

Reaction conditions for the synthesis of thioamide, amidoxime, and N-substituted amidine analogs of the peptide bond are described. Several new amidine analogs of the chemotactic peptide f-Met-Leu-Phe-OR were synthesized using the thioamides as precursors. The assignment of the E/Z configuration was accomplished by nuclear magnetic resonance. The biological activity of these analogs is briefly described.

Virus-Like Particles in a Human Breast Cancer: Structural Similarity to Previously Reported Particles

1973 ◽  
Vol 31 ◽  
pp. 378-379
Author(s):  
G. Kasnic ◽  
S. E. Stewart ◽  
C. Urbanski
Keyword(s):  
Breast Cancer ◽  
Biological Activity ◽  
Human Breast Cancer ◽  
Osteogenic Sarcoma ◽  
Human Tumor ◽  
Structural Similarity ◽  
Cell Tumor ◽  
Human Breast ◽  
Human Tumor Cell ◽  
Type Particle

We have reported the maturation of an intracisternal A-type particle in murine plasma cell tumor cultures and three human tumor cell cultures (rhabdomyosarcoma, lung adenocarcinoma, and osteogenic sarcoma) after IUDR-DMSO activation. In all of these studies the A-type particle seems to develop into a form with an electron dense nucleoid, presumably mature, which is also intracisternal. A similar intracisternal A-type particle has been described in leukemic guinea pigs. Although no biological activity has yet been demonstrated for these particles, on morphologic grounds, and by the manner in which they develop within the cell, they may represent members of the same family of viruses.

Effects of Vincristine on Endothelial Microtubules in the Spinal Cord

1976 ◽  
Vol 34 ◽  
pp. 58-59
Author(s):  
John L. Beggs ◽  
John D. Waggener ◽  
Wanda Miller
Keyword(s):  
Spinal Cord ◽  
Biological Activity ◽  
Horseradish Peroxidase ◽  
Transport Mechanism ◽  
Vasogenic Edema ◽  
Vesicular Transport ◽  
Close Proximity

Microtubules (MT) are versatile organelles participating in a wide variety of biological activity. MT involvement in the movement and transport of cytoplasmic components has been well documented. In the course of our study on trauma-induced vasogenic edema in the spinal cord we have concluded that endothelial vesicles contribute to the edema process. Using horseradish peroxidase as a vascular tracer, labeled endothelial vesicles were present in all situations expected if a vesicular transport mechanism was in operation. Frequently,labeled vesicles coalesced to form channels that appeared to traverse the endothelium. The presence of MT in close proximity to labeled vesicles sugg ested that MT may play a role in vesicular activity.

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