The characterization of the 12 S "globulin" from rapeseed and its glycoprotein component

A 12 S globulin was isolated from each of the two species of rapeseed (B. napus L. and B. campestris L.) and they have been shown to be similar in terms of amino acid composition, amino terminal amino acids, number of subfractions, and carbohydrate content. One of the major proteins, a glycoprotein, present in each of the 12 S aggregates, was isolated and purified. Its amino acid composition, carbohydrate content, N-terminal amino acids, and sedimentation coefficient are reported herein.

Download Full-text

Localization and Characterization of the Cleavage-Associated Neoantigen in the Edomain of Fibrinogen

10.1055/s-0039-1680399 ◽

1977 ◽

Author(s):

E. F. Plow ◽

T. S. Edgington

Keyword(s):

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Conformational Changes ◽

Deae Cellulose ◽

Ion Exchange Chromatography ◽

Exchange Chromatography ◽

Amino Terminal ◽

Exclusion Chromatography

Plasmic cleavage of fibrinogen to generate fragment X partially exposes a specific cryptic molecular site, fg-Eneo. This site in the E domain of the molecule is further exposed during subsequent cleavage. We now report on localization of this site which provides an incisive marker for the structural and conformational changes associated with plasmic cleavage of fibrinogen. Fg-Eneo was stable to reduction and alkylation and the chains of the E fragment were separated by ion exchange chromatography on DEAE-cellulose. An active component was obtained and subjected to molecular exclusion chromatography on Sephadex G-50 to insure removal of intact fg-E. A fg-Eneo positive chain was recovered and identified as Eγ with respect to amino-terminal tyrosine, amino acid composition, and immunochemical analysis. The fg-Eneo site was stable to tryptic degradation, and tryptic peptides were prepared and separated by multiple molecular exclusion chromatographic steps. Final separation of two peptides of similar size was achieved on the basis of carbohydrate content by affinity chromatography on Concanavalin A. Only the active peptide was bound by the lectin. Purity and identification of the active tryptic peptide as γ36–53 was established by amino acid composition and sequence. These results establish that this region of the γ chain of fibrinogen is not present at the hydrated surface of the native molecule but that, in association with plasmic cleavage and conformational changes, this site is progressively exposed and provides a dynamic marker of the cleavage sequence.

Download Full-text

AMINO ACID COMPOSITION AND TERMINAL AMINO ACIDS OF STAPHYLOCOCCAL ENTEROTOXIN B

10.21236/ad0449728 ◽

1964 ◽

Author(s):

Leonard Spero ◽

David Stefanye ◽

Peter I. Brecher ◽

Henry M. Jacoby ◽

Edward J. Schantz

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Staphylococcal Enterotoxin ◽

Staphylococcal Enterotoxin B ◽

Terminal Amino ◽

Enterotoxin B

Download Full-text

Poly(ADP-ribose) polymerase from Ehrlich ascites-tumour cells. Amino acid composition, N-terminal analysis and chemical cleavage of the purified protein

Biochemical Journal ◽

10.1042/bj1850779 ◽

1980 ◽

Vol 185 (3) ◽

pp. 779-782 ◽

Cited By ~ 11

Author(s):

J Holtlund ◽

T Kristensen ◽

K Sletten

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Ascites Tumour ◽

Ehrlich Ascites ◽

Ehrlich Ascites Tumour ◽

Terminal Amino ◽

Ascites Tumour Cells ◽

Ehrlich Ascites Tumour Cells

Poly(ADP-ribose) polymerase was purified from Ehrlich ascites-tumour cells by two novel methods. Analysis for amino acid composition revealed a high percentage of acidic amino acids or their amides, and of basic amino acids. N-Terminal analysis with dansyl chloride revealed no terminal amino acid, indicating a blocked N-terminal amino group. Analysis by gel electrophoresis of protein treated with 3-bromo-3-methyl-2-[(2-nitrophenylthio)-3H-indole, under conditions where selective cleavage of the polypeptide chain at tryptophan residues is obtained, showed six major peptide bands.

Download Full-text

Human pituitary thyrotropin. Isolation and characterization of the hormone and its subunits

Canadian Journal of Biochemistry ◽

10.1139/o77-107 ◽

1977 ◽

Vol 55 (7) ◽

pp. 747-754 ◽

Cited By ~ 10

Author(s):

M. R. Sairam ◽

Choh Hao Li

Keyword(s):

Biological Activity ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Disc Electrophoresis ◽

Carbohydrate Content ◽

Human Pituitary ◽

Terminal Residue ◽

Isolation And Characterization

Procedures have been described for the isolation of highly purified thyrotropin from frozen or acetone-preserved glands or from side fractions of somatotropin isolation and for the separation of its α and β subunits. The products have been characterized by terminal residue analyses, amino acid composition, carbohydrate content, disc electrophoresis, ultracentrifugation, and biological activity.

Download Full-text

Isolation and preliminary biochemical characterization of the gonococcal H.8 antigen.

Journal of Experimental Medicine ◽

10.1084/jem.164.6.2038 ◽

1986 ◽

Vol 164 (6) ◽

pp. 2038-2048 ◽

Cited By ~ 10

Author(s):

W Strittmatter ◽

P J Hitchcock

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Amino Acid Composition ◽

Acid Composition ◽

Preliminary Analysis ◽

Chemical Nature ◽

Biochemical Characterization ◽

Sulfur Containing ◽

Lipid Components

We have presented a method for the extraction and isolation of the gonococcal H.8 antigen. There was no evidence of contamination by other gonococcal proteins, phospholipids, or LPS. The purified H.8 antigen was subjected to preliminary analysis and appeared to be a proteolipid consisting of both protein and lipid components. The amino acid composition was unusual; the peptide portion of the antigen was an alanine and proline-rich molecule that lacked aromatic and sulfur-containing amino acids. The overall amino acid composition is hydrophobic. A lipid constituent was also identified; it was made up of at least two lipid components, which were unique to the H.8 molecule. The chemical nature of the association of the protein and lipid is presently unknown, but it is clearly a tenacious one.

Download Full-text