scholarly journals Comparison of Some Microfibrillar Proteins From Wool

1979 ◽  
Vol 32 (5) ◽  
pp. 437 ◽  
Author(s):  
Lyndsay M Dowling ◽  
Keith H Gough ◽  
Adam S Inglis ◽  
Lindsay G Sparrow
Keyword(s):  
Amino Acid ◽  
Sequence Homology ◽  
Amino Acid Sequences ◽  
Molecular Properties ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Sequence Homologies ◽  
Sulfur Protein ◽  
Low Sulfur ◽  
Similar Amino Acid

The molecular properties of components 5 and 7c, two low-sulfur proteins from the microfibril of wool, have been compared. These proteins have almost identical molecular weights and very similar amino acid compositions. Comparison of the partial amino acid sequences determined to date show extensive regions of sequence homology. No such sequence homologies are observed when these components are compared with component 8c-1, another low-sulfur protein from wool.

scholarly journals THE PURIFICATION AND PARTIAL CHARACTERIZATION OF SEVERAL FORMS OF HOG RENIN SUBSTRATE

1963 ◽  
Vol 118 (1) ◽  
pp. 73-98 ◽  
Author(s):  
Leonard T. Skeggs ◽  
Kenneth E. Lentz ◽  
Harry Hochstrasser ◽  
Joseph R. Kahn
Keyword(s):  
Sialic Acid ◽  
Amino Acid ◽  
Physical Properties ◽  
Deae Cellulose ◽  
Angiotensin I ◽  
Renin Substrate ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Similar Amino Acid

Hog renin substrate has been separated into three major (A, B, and C) and two minor forms (D and E) by DEAE cellulose chromatography. Two of the major forms (B and C) have been further fractionated into two additional types (1 and 2) by countercurrent distribution. The purification of substrates A, C1, and C2 has been completed. Analysis shows that all three are glycoproteins with molecular weights of about 57,000, and have similar amino acid compositions. Differences exist in the sialic acid, glucosamine, and neutral hexose content, which may account for different physical properties. All the forms of the substrates are attacked by renin at similar rates, and appear to yield the same angiotensin I.

scholarly journals The Proteins of the Keratin Component of Bird?s Beaks

1976 ◽  
Vol 29 (6) ◽  
pp. 467 ◽  
Author(s):  
MJ Frenkel ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Major Protein ◽  
Major Fraction ◽  
Amino Acid Compositions ◽  
Molecular Weights ◽  
Isoelectric Points ◽  
Related Proteins ◽  
Keratin Proteins ◽  
Similar Amino Acid

Birds' beaks have an outer shell of hard keratin which consists almost entirely of proteins which are very rich in glycine [about 30 residues per 100 residues (residues %)], contain moderate levels of tyrosine and serine (each about 8 residues %), and which have relatively low contents of cystine (about 2�5 residues %), lysine, histidine, isoleucine and methionine. Major protein fractions in the S-carboxymethyl form isolated from the beaks of 'six different orders of birds have similar amino acid compositions, isoelectric points (pH 4�2-4�9) and molecular weights (13 000--14 500). Detailed chromatographic electrophoretic and compositional studies of the proteins of kookaburra beak reveal them to be a family of closely related proteins with only limited heterogeneity, in contrast to mammalian keratin systems. The major kookaburra beak fraction is similar in overall composition and molecular weight to fowl epidermal scale, kookaburra claw and turtle scute proteins and shows some resemblance to reptile claw protein. Beaks also contain small amounts of protein which are distinctly different from the major fraction but which resemble feather keratin proteins in composition and size.

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.

scholarly journals The Possibility of Common Amino Acid Sequences in High-Sulphur Protein Fractions from Wool

1969 ◽  
Vol 22 (5) ◽  
pp. 1197 ◽  
Author(s):  
RL Darskus ◽  
JM Gillespie ◽  
H Lindley
Keyword(s):  
Amino Acid ◽  
High Voltage ◽  
Paper Electrophoresis ◽  
Structural Features ◽  
Amino Acid Sequences ◽  
Protein Fractions ◽  
Common Amino Acid ◽  
Amino Acid Compositions ◽  
Merino Wool ◽  
Derivatives Of

S-Carboxymethyl derivatives of the high-sulphur components of reduced Merino wool have been subdivided by chromatography into 17 fractions, the amino acid compositions of which are reported. Tryptic, chymotryptic, and thermolysin digests of each fraction have been studied by high-voltage paper electrophoresis at pH 3�5 and 6�5. The results suggest that the high-sulphur proteins consist of families of proteins probably containing common structural features. Evidence is presented that the heterogeneity of high-sulphur proteins is not artefactual.

scholarly journals α-Crystallin. Fractionation of subunits and sequence studies on an isolated polypeptide

1971 ◽  
Vol 124 (2) ◽  
pp. 345-355 ◽  
Author(s):  
Robert C. Augusteyn ◽  
Abraham Spector
Keyword(s):  
Amino Acid ◽  
Gel Electrophoresis ◽  
Cyanogen Bromide ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Iodoacetic Acid ◽  
Cysteine Residue ◽  
Terminal Sequence ◽  
Amino Acid Compositions ◽  
Molecular Weights

α-Crystallin was carboxymethylated with radioactive iodoacetic acid in the presence of 7.6m-urea and then separated into six major fractions by chromatography on DEAE-cellulose in 7m-urea. Based on the amino acid compositions, specific radioactivities and sodium dodecyl sulphate–gel electrophoresis of the fractions, it was concluded that α-crystallin contains at least four different subunits: DU1A and DU1B, containing no cysteine; a third component represented by DU2B and DU3 containing one cysteine one cysteine residue per subunit; and DU4, which probably contains two residues of cysteine per subunit. Subunit DU1A was shown to be of sufficient purity for sequence studies. Cyanogen bromide cleavage yielded two peptides, CB-1 and CB-2, in approximately equal amounts as expected. The sum of the molecular weights and amino acid compositions of the peptides were both in excellent agreement with the results obtained for subunit DU1A. The amino acid sequence of the first sixteen residues of peptide CB-1 is: Ser-Leu-Thr-Lys-Asp-Phe-Asp-Glu-Val-Asn-Ile-Asp-Val-Ser-His-Phe-. The sequence of the first seventeen residues of peptide CB-2 is: Asp-Ile-Ala-Ile-Ser-His-Pro-Trp-Ile-Arg-Pro-Ser-Phe-Phe-Glu-Phe-His-. The N-terminal sequence of subunit DU1A was shown to be N-acetylmethionine followed by peptide CB-2.

Polypeptide chains with similar amino acid sequences but a distinctly different conformation

FEBS Letters ◽  
1983 ◽  
Vol 164 (1) ◽  
pp. 25-27 ◽  
Author(s):  
Bauke W. Dijkstra ◽  
Wicher J. Weijer ◽  
Rik K. Wierenga
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequences ◽  
Polypeptide Chains ◽  
Similar Amino Acid
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