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.

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.

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

Molecular analysis of nuc-1+, a gene controlling phosphorus acquisition in Neurospora crassa

1990 ◽  
Vol 10 (11) ◽  
pp. 5839-5848
Author(s):  
S Kang ◽  
R L Metzenberg
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Phosphorus Acquisition ◽  
Regulatory Factor ◽  
Physical Interactions ◽  
Negative Regulatory Factor ◽  
High Phosphate

In response to phosphorus starvation, Neurospora crassa makes several enzymes that are undetectable or barely detectable in phosphate-sufficient cultures. The nuc-1+ gene, whose product regulates the synthesis of these enzymes, was cloned and sequenced. The nuc-1+ gene encodes a protein of 824 amino acids with a predicted molecular weight of 87,429. The amino acid sequence shows homology with two yeast proteins whose functions are analogous to that of the NUC-1 protein. Two nuc-1+ transcripts of 3.2 and 3.0 kilobases were detected; they were present in similar amounts during growth at low or high phosphate concentrations. The nuc-2+ gene encodes a product normally required for NUC-1 function, and yet a nuc-2 mutation can be complemented by overexpression of the nuc-1+ gene. This implies physical interactions between NUC-1 protein and the negative regulatory factor(s) PREG and/or PGOV. Analysis of nuc-2 and nuc-1; nuc-2 strains transformed by the nuc-1+ gene suggests that phosphate directly affects the level or activity of the negative regulatory factor(s) controlling phosphorus acquisition.

scholarly journals Molecular analysis of nuc-1+, a gene controlling phosphorus acquisition in Neurospora crassa.

1990 ◽  
Vol 10 (11) ◽  
pp. 5839-5848 ◽  
Author(s):  
S Kang ◽  
R L Metzenberg
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Neurospora Crassa ◽  
Phosphorus Acquisition ◽  
Regulatory Factor ◽  
Physical Interactions ◽  
Negative Regulatory Factor ◽  
High Phosphate

In response to phosphorus starvation, Neurospora crassa makes several enzymes that are undetectable or barely detectable in phosphate-sufficient cultures. The nuc-1+ gene, whose product regulates the synthesis of these enzymes, was cloned and sequenced. The nuc-1+ gene encodes a protein of 824 amino acids with a predicted molecular weight of 87,429. The amino acid sequence shows homology with two yeast proteins whose functions are analogous to that of the NUC-1 protein. Two nuc-1+ transcripts of 3.2 and 3.0 kilobases were detected; they were present in similar amounts during growth at low or high phosphate concentrations. The nuc-2+ gene encodes a product normally required for NUC-1 function, and yet a nuc-2 mutation can be complemented by overexpression of the nuc-1+ gene. This implies physical interactions between NUC-1 protein and the negative regulatory factor(s) PREG and/or PGOV. Analysis of nuc-2 and nuc-1; nuc-2 strains transformed by the nuc-1+ gene suggests that phosphate directly affects the level or activity of the negative regulatory factor(s) controlling phosphorus acquisition.

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.

The amino acid sequence of human sperm protamine P1

1985 ◽  
Vol 5 (5) ◽  
pp. 383-391 ◽  
Author(s):  
D. J. McKay ◽  
B. S. Renaux ◽  
G. H. Dixon
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gas Phase ◽  
Human Sperm ◽  
Calculated Molecular Weight ◽  
Phase Protein ◽  
Protein Sequencer

Human sperm protamines have been extracted from spermatozoa pooled from several donors, converted to their S-pyridylethylated derivatives and resolved into two major components, P1 and PI, by Bio-Rex 70 chromatography. Protamine P1 was further purified by Bio-Gel P-10 chromatography and sequenced directly on a gas phase protein sequencer for 43 residues. To complete the sequence, P1 was cleaved at methionine 36 and the C-terminal tetradecapeptide was purified by h.p.i.c, and sequenced completely. The 50 residue sequence is: 10 20 30 40 ARYRC CRSQS RSRYY RQRQR SRRRR RRSCQ TRRRA MRCCR 50 PRYRP RCRRH. This sequence has a calculated molecular weight of 6674 and is homologous with four other published mammalian protamine sequences.

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