scholarly journals Studies on the high-sulphur proteins of reduced Merino wool. Amino acid sequence of protein SCMKB-IIIB4

1971 ◽  
Vol 123 (2) ◽  
pp. 201-210 ◽  
Author(s):  
L. S. Swart ◽  
T. Haylett
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Complete Amino Acid Sequence ◽  
Merino Wool ◽  
The Third ◽  
Wool Proteins

The complete amino acid sequence of protein SCMKB-IIIB4 is presented. It is closely related to the sequence of protein SCMKB-IIIB3 (Haylett, Swart & Parris, 1971) differing in only four positions. The peptic and thermolysin peptides of protein SCMKB-IIIB4 were analysed by the dansyl–Edman method (Gray, 1967) and by tritium-labelling of C-terminal residues (Matsuo, Fujimoto & Tatsuno, 1966). This protein is the third member of a group of high-sulphur wool proteins with molecular weight of about 11400. It consists of 98 residues and has acetylalanine and carboxymethylcysteine as N- and C-terminal residues respectively.

scholarly journals The complete amino acid sequence of the low molecular weight cytosolic acid phosphatase

1989 ◽  
Vol 264 (5) ◽  
pp. 2560-2567
Author(s):  
G Camici ◽  
G Manao ◽  
G Cappugi ◽  
A Modesti ◽  
M Stefani ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Acid Phosphatase ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Low Molecular Weight ◽  
Complete Amino Acid Sequence

scholarly journals Primary structure of bovine complement activation fragment C4a, the third anaphylatoxin. Purification and complete amino acid sequence

1982 ◽  
Vol 207 (2) ◽  
pp. 253-260 ◽  
Author(s):  
M A Smith ◽  
L M Gerrie ◽  
B Dunbar ◽  
J E Fothergill
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Gel Filtration ◽  
Complete Amino Acid Sequence ◽  
The Third ◽  
Human Sequence ◽  
Bovine Plasma ◽  
Bovine Sequence ◽  
C 50

Purification of C4a from heat-activated bovine plasma by elution from CM-Sephadex C-50 at pH 7.4 and gel filtration on Sephadex G-50 gives a 20% yield of pure C4a. The complete amino acid sequence of bovine C4a has been determined by automatic sequencer degradation of CNBr and enzymic fragments, and by carboxypeptidase digestion. The 77-residue bovine sequence shows 12 differences from the human sequence with five of these differences occurring in the C-terminal 11 residues. The sequence of C4a confirms earlier suggestions of homology with C3a and C5a: the three sequences show an almost equal number of identities with each other. The six cysteine residues of the ‘disulphide knot’ are conserved as well as seven other residues including the C-terminal arginine.

Studies on the High-Sulfur Proteins of Reduced Merino Wool

1969 ◽  
Vol 39 (10) ◽  
pp. 917-929 ◽  
Author(s):  
T. Haylett ◽  
L. S. Swart
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Proteolytic Enzymes ◽  
Deae Cellulose ◽  
Notable Feature ◽  
Merino Wool ◽  
Amino Terminal ◽  
Sulfur Protein ◽  
Low Sulfur

The first complete amino-acid sequence of a wool protein is presented. The high-sulfur protein SCMKB-IIIB2, with a molecular weight of 11,260, consists of 97 residues and has an acetylated amino terminal. A notable feature of the protein is that it has a high- and a low-sulfur region. The sequence was determined by examination of the peptides released by various proteolytic enzymes and separated by chromatography on DEAE-cellulose with volatile buffers.

A Gastric Inhibitory Polypeptide II: The Complete Amino Acid Sequence

1971 ◽  
Vol 49 (8) ◽  
pp. 867-872 ◽  
Author(s):  
John C. Brown ◽  
Jill R. Dryburgh
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Residue ◽  
Gastric Inhibitory Polypeptide ◽  
Complete Amino Acid Sequence ◽  
Calculated Molecular Weight ◽  
Residue Polypeptide

Porcine gastric inhibitory polypeptide is a 43 amino acid residue polypeptide with the amino acid sequence Tyr–Ala–Glu–Gly–Thr–Phe–Ile–Ser–Asp–Tyr–Ser–Ile–Ala–Met–Asp–Lys–Ile–Arg–Gln–Gln–Asp–Phe–Val–Asn–Trp–Leu–Leu–Ala–Gln–Gln–Lys–Gly–Lys–Lys–Ser–Asp–Trp–Lys–His–Asn–Ile–Thr–Gln. Fifteen of the first 26 amino acids occur in the same position as they do in porcine glucagon, and nine of the first 26 in the same position as in porcine secretin. The calculated molecular weight of the polypeptide is 5105.

Motilin, a Gastric Motor Activity Stimulating Polypeptide: The Complete Amino Acid Sequence

1973 ◽  
Vol 51 (5) ◽  
pp. 533-537 ◽  
Author(s):  
John C. Brown ◽  
Michael A. Cook ◽  
Jill R. Dryburgh
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Motor Activity ◽  
Amino Acid Residue ◽  
Complete Amino Acid Sequence ◽  
Gastric Motor Activity ◽  
Calculated Molecular Weight ◽  
Residue Polypeptide

Porcine motilin is a 22 amino acid residue polypeptide with the amino acid sequence Phe–Val–Pro–Ile–Phe–Thr–Tyr–Gly–Glu–Leu–Gln–Arg–Met–Glu–Glu–Lys–Glu–Arg–Asn–Lys–Gly–Gln. The calculated molecular weight is 2700.

Isolation and Structural Charaderization of a Potent Inhibitor of Coagulation Factor Xa from the Leech Haementeria ghilianii

1989 ◽  
Vol 61 (03) ◽  
pp. 437-441 ◽  
Author(s):  
Cindra Condra ◽  
Elka Nutt ◽  
Christopher J Petroski ◽  
Ellen Simpson ◽  
P A Friedman ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Salivary Gland ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Western Blot ◽  
Potent Inhibitor ◽  
Factor Xa ◽  
Coagulation Factor ◽  
Sds Page ◽  
Bovine Factor

SummaryThe present work reports the discovery and charactenzation of an anticoagulant protein in the salivary gland of the giant bloodsucking leech, H. ghilianii, which is a specific and potent inhibitor of coagulation factor Xa. The inhibitor, purified to homogeneity, displayed subnanomolar inhibition of bovine factor Xa and had a molecular weight of approximately 15,000 as deduced by denaturing SDS-PAGE. The amino acid sequence of the first 43 residues of the H. ghilianii derived inhibitor displayed a striking homology to antistasin, the recently described subnanomolar inhibitor of factor Xa isolated from the Mexican leech, H. officinalis. Antisera prepared to antistasin cross-reacted with the H. ghilianii protein in Western Blot analysis. These data indicate that the giant Amazonian leech, H. ghilianii, and the smaller Mexican leech, H. officinalrs, have similar proteins which disrupt the normal hemostatic clotting mechanisms in their mammalian host’s blood.

Complete Covalent Structure of Human Platelet Factor 4

1979 ◽  
Vol 42 (05) ◽  
pp. 1652-1660 ◽  
Author(s):  
Francis J Morgan ◽  
Geoffrey S Begg ◽  
Colin N Chesterman
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Platelet ◽  
Platelet Factor 4 ◽  
Platelet Factor ◽  
Disulphide Bonds ◽  
Covalent Structure

SummaryThe amino acid sequence of the subunit of human platelet factor 4 has been determined. Human platelet factor 4 consists of identical subunits containing 70 amino acids, each with a molecular weight of 7,756. The molecule contains no methionine, phenylalanine or tryptophan. The proposed amino acid sequence of PF4 is: Glu-Ala-Glu-Glu-Asp-Gly-Asp-Leu-Gln-Cys-Leu-Cys-Val-Lys-Thr-Thr-Ser- Gln-Val-Arg-Pro-Arg-His-Ile-Thr-Ser-Leu-Glu-Val-Ile-Lys-Ala-Gly-Pro-His-Cys-Pro-Thr-Ala-Gin- Leu-Ile-Ala-Thr-Leu-Lys-Asn-Gly-Arg-Lys-Ile-Cys-Leu-Asp-Leu-Gln-Ala-Pro-Leu-Tyr-Lys-Lys- Ile-Ile-Lys-Lys-Leu-Leu-Glu-Ser. From consideration of the homology with p-thromboglobulin, disulphide bonds between residues 10 and 36 and between residues 12 and 52 can be inferred.

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