Chemical characterization of lung surfactant apoproteins: amino acid composition, N-terminal sequence and enzymic digestion

1985 ◽  
Vol 13 (6) ◽  
pp. 1092-1096 ◽  
Author(s):  
SAMUEL HAWGOOD ◽  
HAVA EFRATI ◽  
JAMES SCHILLING ◽  
BRADLEY J. BENSON
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Lung Surfactant ◽  
Chemical Characterization ◽  
Terminal Sequence ◽  
Enzymic Digestion

scholarly journals Amino Acid Composition and Amino-Terminal Sequence of Yeast Enolase

1959 ◽  
Vol 234 (5) ◽  
pp. 1108-1111
Author(s):  
Bo G. Malmström ◽  
J.R. Kimmel ◽  
Emil L. Smith
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Amino Terminal ◽  
Amino Terminal Sequence ◽  
Yeast Enolase

scholarly journals Silkmoth chorion proteins. Their diversity, amino acid composition, and the NH-terminal sequence of one component

1978 ◽  
Vol 253 (4) ◽  
pp. 1305-1314
Author(s):  
J.C. Regier ◽  
F.C. Kafatos ◽  
K.J. Kramer ◽  
R.L. Heinrikson ◽  
P.S. Keim
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Terminal Sequence ◽  
Silkmoth Chorion

Proteins in the Enamel Fluid of Immature Porcine Teeth

1987 ◽  
Vol 66 (12) ◽  
pp. 1721-1726 ◽  
Author(s):  
T. Aoba ◽  
T. Tanabe ◽  
E.C. Moreno
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Protein Content ◽  
Acid Composition ◽  
Permanent Teeth ◽  
Major Protein ◽  
Protein Species ◽  
Terminal Sequence ◽  
Molecular Weights ◽  
Sds Electrophoresis

The fluid was separated from the immature soft enamel of porcine permanent teeth in the secretory stage according to procedures reported previously (Aoba and Moreno, 1987). The protein content of the fluid was about 2.8% w/v; its amino-acid composition was characterized by high contents of Pro, Glx, Leu, and His, showing composition similar to that of the 20 kilo-dalton (kd) amelogenin or its C-terminal segments. The two major protein species in the fluid had apparent molecular weights of 13 kd and 11 kd, as determined by SDS electrophoresis; the N-terminal residue of the former was Leu, while that of the latter was Ala. The C-terminal sequence of both of them was -Met-Phe-Ser. By comparison with the published sequence of 20-kd porcine amelogenin, it is concluded that the main fluid constituents were derived by cleavages of N-terminal segments from the 20-kd amelogenin.

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 Comparative biochemical analysis of lectin and nuclease from Chelidonium majus L.

2000 ◽  
Vol 47 (2) ◽  
pp. 413-420 ◽  
Author(s):  
E Fik ◽  
M Dalgalarrondo ◽  
T Haertlé ◽  
A Goździcka-Józefiak
Keyword(s):  
Amino Acid ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Biochemical Analysis ◽  
Dnase Activity ◽  
Chelidonium Majus ◽  
Terminal Sequence ◽  
Leaves And Roots ◽  
Comparative Biochemical Analysis

It has been recently recognized that lectins exhibit other activities besides hemagglutination. Previously we have found that purified lectin from Chelidonium majus showed DNase activity (Fik, Goździcka-Józefiak & Kedzia, 1995, Herba Polon. 41, 84-95). Comparison of lectin and DNase from the sap from leaves and roots of Chelidonium majus proved that both these compounds are composed of 24 kDa monomer subunits which have an identical N-terminal sequence but differ in amino-acid composition and degree of glycosylation. Possible interrelationship between lectin and DNase is discussed.

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.

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