Biochemical and immunological characterization of rice albumin

1987 ◽  
Vol 7 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Yogesh R. Mawal ◽  
Madhumalti R. Mawal ◽  
P. K. Ranjekar
Keyword(s):  
Oryza Sativa ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Seed Proteins ◽  
Major Fraction ◽  
Con A ◽  
Rf Values ◽  
Total Seed

Rice albumin from Oryza sativa (Var. Basmati 370) accounts for about 5% of the total seed proteins. A major fraction of rice albumin has been found to be a glycoprotein which is a monomer of 60 kd having iso-electric point 6.54. When rice albumin is digested with trypsin, it shows the presence of 24 peptides as against 28 peptides which were estimated from its amino acid Composition. This indicates the presence of a few peptides which resemble each other in their charge and Rf values. Antibodies against Con A purified rice albumin were affinity purified and were used to quantitate the rice albumin levels during post-anthesis by RIA and ELISA. The latter experiments reveal that maximum albumin is present between 18 and 20 days post-anthesis.

scholarly journals Homologies in amino acid composition and structure of histone F2al isolated from human leukaemic cells

1970 ◽  
Vol 119 (2) ◽  
pp. 165-170 ◽  
Author(s):  
Laxman S. Desai ◽  
George E. Foley
Keyword(s):  
Gene Regulation ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Neoplastic Cells ◽  
Amino Acid Compositions ◽  
Composition And Structure ◽  
Leukaemic Cells ◽  
Rf Values ◽  
Similar Amino Acid

Histones F2al extracted from normal and neoplastic cells possess similar amino acid compositions. Tryptic and chymotryptic peptides of the F2al histones have identical chromato-electrophoretic RF values. It is concluded that histones F2al from various sources have similar overall structures. The observed differences in the ratios of ∈-N-monomethyl- and di-∈-N-methyl-lysine in the histones from normal and neoplastic cells may be of significance with respect to gene regulation.

Seed proteins of finger millet and their amino acid composition

1975 ◽  
Vol 26 (8) ◽  
pp. 1237-1246 ◽  
Author(s):  
Tumkur K. Virupaksha ◽  
Geeta Ramachandra ◽  
Dasasetty Nagaraju
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Finger Millet ◽  
Seed Proteins

Amino acid composition of leaf, grain and bracts of japonica rice (Oryza Sativa ssp. japonica) and its response to nitrogen fertilization

2016 ◽  
Vol 82 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Xincheng Zhang ◽  
Jinchao Lei ◽  
Deyi Zheng ◽  
Zhenghui Liu ◽  
Ganghua Li ◽  
...  
Keyword(s):  
Oryza Sativa ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Nitrogen Fertilization ◽  
Japonica Rice

scholarly journals High-Sulphur Proteins From a-Keratins ll. Isolation and Partial Characterization of Purified Components From Mouse Hair

1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fractional Precipitation ◽  
Molecular Weight Range

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.

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

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.

scholarly journals Characterization of Human KAP24.1, A Cuticular Hair Keratin-Associated Protein with Unusual Amino-Acid Composition and Repeat Structure

2007 ◽  
Vol 127 (5) ◽  
pp. 1197-1204 ◽  
Author(s):  
Michael A. Rogers ◽  
Hermelita Winter ◽  
Lutz Langbein ◽  
Anke Wollschläger ◽  
Silke Praetzel-Wunder ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Repeat Structure ◽  
Hair Keratin ◽  
Unusual Amino Acid
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