scholarly journals Selective Degradation by Bromine Water of the Polypeptide Chains of Oxidized Insulin

1960 ◽  
Vol 13 (1) ◽  
pp. 106 ◽  
Author(s):  
EOP Thompson
Keyword(s):  
Performic Acid ◽  
Peptide Fragments ◽  
Single Product ◽  
Bromine Water ◽  
Selective Degradation ◽  
Polypeptide Chains

In degradative work on oxytocin (Mueller, Pierce, and du Vigneaud 1953; Ressler, Trippett, and du Vigneaud 1953; du Vigneaud et al. 1954) it was found that whereas oxidation with performic acid gave a single product (I), oxidation with bromine water or treatment of (I) with bromine water gave two peptide fragments, resulting from cleavage of a dibromotyrosylisoleucyl bond.

BIOLOGICAL ACTIONS OF HUMAN SOMATOTROPHIN AND ITS DERIVATIVES ON MOUSE MAMMARY GLAND AND TELEOST URINARY BLADDER

1977 ◽  
Vol 73 (2) ◽  
pp. 377-383 ◽  
Author(s):  
B. A. DONEEN ◽  
H. A. BERN ◽  
CHOH HAO LI
Keyword(s):  
Mammary Gland ◽  
Urinary Bladder ◽  
Tertiary Structure ◽  
Biological Activities ◽  
Mouse Mammary Gland ◽  
Performic Acid ◽  
Acid Oxidation ◽  
Peptide Fragments ◽  
Ovine Prolactin

SUMMARY These studies are concerned with the structural and functional evolution of the ancestrally related pituitary prolactins and somatotrophins. Prolactin-like biological activities of human somatotrophin (hGH) and its peptide fragments were bioassayed in vitro on the mouse mammary gland and the teleost urinary bladder. Plasmin modified-hGH was as active as hGH in both bioassays. The NH2-terminal 134-residue fragment possessed about 10% of the lactogenic and urinary bladder potency of hGH, whereas the CO2H-terminal 51-residue fragment was inactive at the concentrations observed. These results suggest that the same regions of primary structure are responsible for the prolactin-like actions of hGH on the target organs of lower and higher vertebrates. Alteration of the tertiary structure of hGH, human chorionic somatomammotrophin, and ovine prolactin by performic acid oxidation destroys the mammary gland activities of these hormones.

scholarly journals THE NUMBER OF POLYPEPTIDE CHAINS IN BOVINE PLASMA ALBUMIN

1956 ◽  
Vol 34 (2) ◽  
pp. 160-169 ◽  
Author(s):  
M. E. Reichmann ◽  
J. Ross Colvin
Keyword(s):  
Molecular Weight ◽  
Light Scattering ◽  
Sodium Chloride ◽  
Sedimentation Velocity ◽  
Performic Acid ◽  
Sedimentation Equilibrium ◽  
Plasma Albumin ◽  
Disulphide Bonds ◽  
Bovine Plasma ◽  
Polypeptide Chains

The molecular weight of performic acid oxidized bovine plasma albumin, dispersed in 0.08 M borate +0.2 M sodium chloride buffer, pH 7.4, was estimated as 30,000 by light-scattering and sedimentation equilibrium methods, 19,000 by osmotic pressure. Sedimentation velocity analyses and electrophoresis showed that the component polypeptide chains of the material are similar in mass and charge density so the polydispersity must be attributed to labile aggregates. The results indicate that here are at least three and probably four similar polypeptide chains in the molecule of native bovine plasma albumin, held together by disulphide bonds.

scholarly journals TREATMENT OF PERFORMIC ACID-OXIDIZED OXYTOCIN WITH BROMINE WATER

1953 ◽  
Vol 204 (2) ◽  
pp. 857-860
Author(s):  
Johannes M. Mueller ◽  
John G. Pierce ◽  
Vincent du Vigneaud
Keyword(s):  
Performic Acid ◽  
Bromine Water

scholarly journals Use of octadecasilyl-silica for the extraction and purification of peptides in biological samples. Application to the identification of circulating metabolites of corticotropin-(1-24)-tetracosapeptide and somatostatin in vivo

1977 ◽  
Vol 168 (1) ◽  
pp. 9-13 ◽  
Author(s):  
H P J Bennett ◽  
A M Hudson ◽  
C McMartin ◽  
G E Purdon
Keyword(s):  
Aqueous Solution ◽  
Biological Activity ◽  
Solvent Mixtures ◽  
Plasma Samples ◽  
Peptide Fragments ◽  
Single Product ◽  
Extraction And Purification ◽  
Aqueous Solvent

Peptides can be adsorbed on octadecasilyl-silica from large volumes of aqueous solution and eluted with aqueous solvent mixtures containing methanol or acetonitrile. These properties may be used for the extraction and purification of peptide fragments in plasma samples collected from rats. After intravenous injection of Synacthen [corticotropin-(1-24)-tetracosapeptide], it was shown that within 2 min the main circulating products were intact peptide and its sulphoxide. In addition, a number of fragments indicative of cleavage at the N- and C-termini were present. Most of the products formed from Synacthen have low biological activity. Somatostatin was rapidly cleaved in vivo and in vitro to a single product, which probably retains biological activity. The absence of other circulating products suggests that somatostatin is only inactivated once it leaves the circulation.

Insights into amyloid disease from fly models

2014 ◽  
Vol 56 ◽  
pp. 69-83 ◽  
Author(s):  
Ko-Fan Chen ◽  
Damian C. Crowther
Keyword(s):  
Drosophila Melanogaster ◽  
Neurodegenerative Disorders ◽  
Amyloid Β ◽  
Amyloid Β Peptide ◽  
Disease Pathogenesis ◽  
Amyloid Aggregates ◽  
Aβ Amyloid ◽  
Polypeptide Chains ◽  
Amyloid Diseases

The formation of amyloid aggregates is a feature of most, if not all, polypeptide chains. In vivo modelling of this process has been undertaken in the fruitfly Drosophila melanogaster with remarkable success. Models of both neurological and systemic amyloid diseases have been generated and have informed our understanding of disease pathogenesis in two main ways. First, the toxic amyloid species have been at least partially characterized, for example in the case of the Aβ (amyloid β-peptide) associated with Alzheimer's disease. Secondly, the genetic underpinning of model disease-linked phenotypes has been characterized for a number of neurodegenerative disorders. The current challenge is to integrate our understanding of disease-linked processes in the fly with our growing knowledge of human disease, for the benefit of patients.

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

1999 ◽  
Vol 96 (9/10) ◽  
pp. 1580-1584 ◽  
Author(s):  
I. Ségalas ◽  
S. Desjardins ◽  
H. Oulyadi ◽  
Y. Prigent ◽  
S. Tribouillard ◽  
...  
Keyword(s):  
Dna Binding ◽  
Binding Domain ◽  
Dna Binding Domain ◽  
Peptide Fragments ◽  
Nmr Studies ◽  
Related Peptide

Common Antigenic Sites in Human, Bovine and Porcine Fibrinogens

1981 ◽  
Vol 45 (02) ◽  
pp. 169-172 ◽  
Author(s):  
Czeslaw S Cierniewski
Keyword(s):  
Antigenic Determinants ◽  
Antigenic Sites ◽  
Specific Antisera ◽  
Antigenic Homology ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

SummarySpecific antisera to the Aα, Bβ and γ chains of porcine fibrinogen were used to characterize an antigenic homology of human, bovine, and porcine fibrinogens. Antigenic determinants shared by these fibrinogens were mostly formed by the Aα chain. However, in the case of bovine and porcine fibrinogens they were also found in the Bβ and γ polypeptide chains. The results reported here show that the Aα chain determinants exposed on the intact fibrinogen molecule are conserved to a considerably larger extent than those of the Bβ and γ chains.

Sialic Acid Dependent Polypeptide Chain Heterogeneity of Human Fibrinogen Demonstrated by Two-Dimensional Electrophoresis

1982 ◽  
Vol 47 (01) ◽  
pp. 019-021 ◽  
Author(s):  
Cemal Kuyas ◽  
André Haeberli ◽  
P Werner Straub
Keyword(s):  
Sialic Acid ◽  
Polypeptide Chain ◽  
Two Dimensional ◽  
Charge Heterogeneity ◽  
Human Fibrinogen ◽  
Two Dimensional Electrophoresis ◽  
Isoelectric Points ◽  
Polypeptide Chains ◽  
Dimensional Electrophoresis ◽  
Chain Type

SummaryHuman fibrinogen was compared with asialofibrinogen by two-dimensional electrophoresis to evaluate the contribution of sialic acid to the heterogeneity of the γ- and Bβ-polypeptide chains.Reduced fibrinogen showed three major variants for both the γ- and Bβ-chains. In addition two minor γ-bands with a more acidic isoelectric point than the normal γ-chains were observed. Electrophoresis in the second dimension (SDS) suggests that these most acidic bands are γ-chain-variants with a higher molecular weight. In asialofibrinogen only two predominant variants with more alkaline isoelectric points were present in each chain type.It is concluded that enzymatic removal of sialic acid partially reduces the heterogeneity of the γ- and Bβ-polypeptide chains of human fibrinogen, but additional sources producing charge heterogeneity must be sought.

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