scholarly journals Amino acid sequence and biological activity of a calcitonin-like diuretic hormone (DH31) from Rhodnius prolixus

2008 ◽  
Vol 211 (3) ◽  
pp. 382-390 ◽  
Author(s):  
V. A. T. Brugge ◽  
D. A. Schooley ◽  
I. Orchard
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Rhodnius Prolixus ◽  
Diuretic Hormone

Complete Amino Acid Sequence of Globin Chains and Biological Activity of Fragmented Crocodile Hemoglobin (Crocodylus siamensis)

2012 ◽  
Vol 31 (6) ◽  
pp. 466-476 ◽  
Author(s):  
Saowaluck Srihongthong ◽  
Anawat Pakdeesuwan ◽  
Sakda Daduang ◽  
Tomohiro Araki ◽  
Apisak Dhiravisit ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Globin Chains ◽  
Crocodylus Siamensis

Amino acid sequence of piratoxin-I, a myotoxin fromBothrops pirajai snake venom, and its biological activity after alkylation withp-bromophenacyl bromide

1998 ◽  
Vol 17 (7) ◽  
pp. 713-718 ◽  
Author(s):  
Marcos H. Toyama ◽  
Andreimar M. Soares ◽  
Carlos A. Vieira ◽  
José C. Novello ◽  
Benedito Oliveira ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Snake Venom

Mass spectrometry analysis, amino acid sequence and biological activity of venom components from the Brazilian scorpion Opisthacanthus cayaporum

Toxicon ◽  
2008 ◽  
Vol 51 (8) ◽  
pp. 1499-1508 ◽  
Author(s):  
Elisabeth F. Schwartz ◽  
Thalita S. Camargos ◽  
Fernando Z. Zamudio ◽  
Luciano P. Silva ◽  
Carlos Bloch ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

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.

Weitere Untersuchungen zur Aminosäuresequenz des Melittins

1969 ◽  
Vol 24 (1) ◽  
pp. 33-35 ◽  
Author(s):  
Joachim Jentsch
Keyword(s):  
Aqueous Solution ◽  
Molecular Weight ◽  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Optical Rotatory Dispersion ◽  
Optical Rotatory ◽  
Surface Active ◽  
Α Helix

Melittin is the (main) toxic peptide of bee venom having a molecular weight of 2840, with a known sequence (s. fig. 1). Optical rotatory dispersion of non-crystalline melittin in aqueous solution suggests that the polypeptide chain is random, although 7% α-helix has been determined. These results are in agreement with the amino acid sequence of melittin and the assumption that the biological activity is attributable to its surface active character.

Sign in / Sign up

Export Citation Format

Share Document