Characterization of the cleavage products of human serum immunoglobulin disulphide bonds. II. S-Cyano derivatives

1967 ◽  
Vol 20 (6) ◽  
pp. 1265 ◽  
Author(s):  
CJ Brackenridge
Keyword(s):  
Amino Acid ◽  
Human Serum ◽  
Native Protein ◽  
Terminal Amino Acid ◽  
Disulphide Bonds ◽  
Exclusion Chromatography ◽  
Terminal Amino ◽  
Oxidative Sulphitolysis ◽  
Polypeptide Chains

The displacement by cyanide ions of S-sulpho substituents from sulphitolysed human serum immunoglobulins yielded S-cyano derivatives, the solubility and sedimentation characteristics of which were examined with respect to pH. Exclusion chromatography gave rise to an aggregated and an unaggregated fraction in proportions similar to those found after oxidative sulphitolysis. Evidence obtained from immunoelectrophoresis, N-terminal amino acid assay, and hexose and amino acid analysis showed that both S-cyano fractions contained polypeptide chains in the same ratios as in the native protein.

Characterization of the cleavage products of human serum immunoglobulin disulphide bonds. I. S-Sulpho derivatives

1967 ◽  
Vol 20 (6) ◽  
pp. 1243 ◽  
Author(s):  
CJ Brackenridge
Keyword(s):  
Human Serum ◽  
Serum Immunoglobulin ◽  
Amino Terminal ◽  
Disulphide Bonds ◽  
Exclusion Chromatography ◽  
Polypeptide Chains ◽  
Antibody Interactions ◽  
Dispersing Agents ◽  
Time Of Reaction

An examination of variables, including amount of catalyst, pH, sulphite concentration, specific buffer salts, and time of reaction led to conditions for the quantitative sulphitolysis of human serum immunoglobulin disulphide bonds. The cleavage was carried out in the absence of dispersing agents, using air as oxidant and cupric ions as catalyst. The treated protein was characterized by solubility, exclusion chromatography, ultracentrifugation, and immunoelectrophoresis. Separation into three fractions of different molecular weight was achieved by passage through Sephadex G-200 gel. Efforts to eliminate the proportion of aggregated material, which showed no tendency to establish an equilibrium with the remaining two unaggregated fractions, were largely unsuccessful. It was concluded that non-covalent forces play a significant role in antibody interactions. The isolated fractions were individually characterized by sedimentation, heat precipitation, immunoelectrophoresis, and quantitative analysis of amino-terminal residues. This led to the demonstration of at least two polypeptide chains present in each fraction.

PURIFICATION AND PARTIAL CHEMICAL CHARACTERIZATION OF SHEEP NEUROPHYSIN

1973 ◽  
Vol 74 (2) ◽  
pp. 226-236 ◽  
Author(s):  
Michel Chrétien ◽  
Claude Gilardeau
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Chemical Characterization ◽  
Terminal Amino Acid ◽  
Amino Acid Determination ◽  
Pituitary Glands ◽  
Terminal Amino ◽  
Partial Chemical ◽  
Acid Determination

ABSTRACT A protein isolated from ovine pituitary glands has been purified, and its homogeneity assessed by NH2- and COOH-terminal amino acid determination, ultracentrifugation studies, and polyacrylamide gel electrophoresis after carboxymethylation. Its chemical and immunochemical properties are closely similar to those of beef and pork neurophysins, less similar to those of human neurophysins. It contains no tryptophan (like other neurophysins) or histidine (like all except bovine neurophysin-I and human neurophysins). It has alanine at the NH2-terminus and valine at the COOH-terminus. Its amino acid composition is similar to, but not identical with those of porcine and bovine neurophysins.

scholarly journals Purification and partial characterization of a lectin from Caesalpinia tinctoria Domb, ex Dc fruits

2003 ◽  
Vol 15 (2) ◽  
pp. 119-122 ◽  
Author(s):  
Marli Lourdes de Oliveira ◽  
Leila Maria Beltramini ◽  
Salvatore Giovanni de Simone ◽  
Maria Helena Nasser Brumano ◽  
Rosemeire Aparecida Silva-Lucca ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Terminal Amino Acid ◽  
Saline Extract ◽  
Hydrophobic Residues ◽  
Terminal Amino ◽  
Helix Conformation ◽  
Far Ultraviolet ◽  
Terminal Amino Acid Sequence

A lectin was isolated from the pod saline extract of Caesalpinia tinctoria by dialoconcentration on Centripep-10 and affinity chromatography on chitin column. The purified lectin was partially characterized with respect to its biochemical and structural properties. It contains 8.3 % of carbohydrate and exhibited an agglutinating activity against human erythrocytes (ABO groups). Its amino acid composition was characterized by a great number of acidic and hydrophobic residues and the estimated molecular mass was 12.5 kDa. The presence of only one N-terminal amino acid sequence (D¹-V-P-A-Y-V-Y-V-H-F10-G-F-G-E-E-H-R -D-V-F20-D), showed the homogeneity of the purified lectin. The far-ultraviolet circular dichroism (CD) spectrum of lectin indicated that it contains 10 % a-helix, 38 % b-sheet, 28 % unordered form and 6 % of P II (poly-L-proline II helix conformation).

Existence of Common Antigenic Determinants in the Aα, Bβ and γ Chains of Some Mammalian Fibrinogens.

1979 ◽  
Author(s):  
C.S. Cierniewski
Keyword(s):  
Amino Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Polyacrylamide Gel ◽  
Antigenic Determinants ◽  
Terminal Amino Acid ◽  
Human Fibrinogen ◽  
Passive Hemagglutination ◽  
Terminal Amino ◽  
Polypeptide Chains ◽  
Fibrinogen Molecule

Polypeptide chains Aα, Bβ and γ of porcine fibrinogen were isolated by preparative SDS polyacrylamide gel electrophoresis. Their purity was estimated by electrophoresis in polyacrylamide gel, amino acid composition and N-terminal amino acid analyses. Antisera to the pig polypeptide chains were produced in rabbits and they were employed in immunological comparative studies of porcine, bovine, human and duck fibrinogens. Antisera to the pig Aα chain showed in gel immunodiffusion and passive hemagglutination a strong cross-reaction with porcine, bovine and human fibrinogens. Antisera to the pig βB and γ chains cross-reacted only with porcine and bovine fibrinogens but they did not recognize human fibrinogen, The reaction of antiγ antisera was detectable only by passive hemagglutination test. In all cases antigenic similarity of the analyzed fibrinogens was mainly related to antigenic determinants of the Aα, Bβ and γ chains exposed on the intact fibrinogen molecule. None of analyzed antisera reacted with duck fibrinogen.

Isolation and characterization of β-lipolytic hormone from porcine pituitary gland

1970 ◽  
Vol 48 (9) ◽  
pp. 1017-1021 ◽  
Author(s):  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Pituitary Gland ◽  
Amino Acid Composition ◽  
Biological Activities ◽  
Terminal Amino Acid ◽  
Isolation And Characterization ◽  
Pituitary Glands ◽  
Terminal Amino

A lipolytic substance was isolated from porcine pituitary glands. It's amino acid composition, molecular weight, N-terminal amino acid, isoelectric point, and biological activities are reported. These results are compared to the corresponding values of sheep β-lipolytic hormone.

Expression of recombinant proteins lacking methionine as N-terminal amino acid in plastids: Human serum albumin as a case study

2007 ◽  
Vol 127 (4) ◽  
pp. 593-604 ◽  
Author(s):  
Alicia Fernández-San Millán ◽  
Inmaculada Farran ◽  
Andrea Molina ◽  
Angel M. Mingo-Castel ◽  
Jon Veramendi
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Recombinant Proteins ◽  
Terminal Amino Acid ◽  
Terminal Amino
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