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.

scholarly journals Amino acid sequence of versutoxin, a lethal neurotoxin from the venom of the funnel-web spider Atrax versutus

1988 ◽  
Vol 250 (2) ◽  
pp. 401-405 ◽  
Author(s):  
M R Brown ◽  
D D Sheumack ◽  
M I Tyler ◽  
M E H Howden
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Gas Phase ◽  
Edman Degradation ◽  
Amino Acid Residues ◽  
Single Chain ◽  
Male And Female ◽  
Web Spider ◽  
Phase Protein ◽  
Protein Sequencer

The complete amino acid sequence of versutoxin, a lethal neurotoxic polypeptide isolated from the venom of male and female funnel-web spiders of the species Atrax versutus, was determined. Sequencing was performed in a gas-phase protein sequencer by automated Edman degradation of the S-carboxymethylated toxin and fragments of it produced by reaction with CNBr. Versutoxin consisted of a single chain of 42 amino acid residues. It was found to have a high proportion of basic residues and of cystine. The primary structure showed marked homology with that of robustoxin, a novel neurotoxin recently isolated from the venom of another funnel-web-spider species, Atrax robustus.

Determination of Low Molecular weight Immunogenic Omp28 Protein and Gene of Salmonella typhimurium

2019 ◽  
Vol 8 (5) ◽  
pp. 172-177
Author(s):  
Rajeev Kumar ◽  
S. P. Singh ◽  
Mahesh Kumar ◽  
Anil Kumar
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Outer Membrane ◽  
Close Agreement ◽  
Outer Membrane Proteins ◽  
Low Molecular Weight ◽  
Predicted Amino Acid Sequence ◽  
Calculated Molecular Weight ◽  
Amplicon Size

Outer membrane of Gram-negative bacteria has complex profile of proteins. The outer membrane proteins (OMPs) isolated from S. typhimurium by urea-EDTA extraction method and analysed through SDS-PAGE showed a complex electrophoretic profile having more than 15 low molecular weight proteins with molecular masses ranging between 3.5 and 43 kDa. The most important outer membrane protein (Omp28) of S. typhimurium with submolecular masses of 12.32kDa of main protein was recovered. The gene responsible for expression of this protein was also amplified through PCR and sequenced, showed 341bp amplicon size and predicted amino acid sequence of this pro-tein was determined. The Antigenic index was calculated from amino acid sequence of same gene and found 2.2 (0.1-2.2) suggesting highly antigenic in nature. The experimentally determined values are close agreement with the theoretically calculated molecular weight 12.32 kDa and pI: 9.61 from the gene sequence of this protein. The antigenic natures of predicted protein values are close agreement with experimental determent of Omp28 of S. typhimurium a possible formula for vaccine developmental of genus Salmonella.

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.

scholarly journals Characterization of cry1Cb3 and cry1Fb7 from Bacillus thuringiensis subsp. galleriae

2015 ◽  
Vol 10 (1) ◽  
Author(s):  
Tianpei Huang ◽  
Ying Xiao ◽  
Jieru Pan ◽  
Lingling Zhang ◽  
Ivan Gelbič ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Bacillus Thuringiensis ◽  
Amino Acid Sequence ◽  
Amino Acid Residues ◽  
Reading Frame ◽  
Bacillus Thuringiensis Subsp ◽  
Calculated Molecular Weight ◽  
Pcr Rflp ◽  
Genes Encoding

AbstractTwo cry1-type genes encoding insecticidal crystal proteins (ICPs) were detected by PCR-RFLP and cloned from Bacillus thuringiensis subsp. galleriae 87. The nucleotide sequences were deposited in GenBank with accession numbers EU679501 and EU679502, and designated as cry1Fb7 and cry1Cb3 respectively by B. thuringiensis Delta- Endotoxin Nomenclature Committee. cry1Cb3 shared 99% homology with other cry1Cb genes. The existence of two additional stop codons indicated cry1Cb3 was a silent gene. The cry1Cb3 was 3531 bp with 38.98% G+C content and its first open reading frame (ORF) encoded a protein of 213 amino acid residues with a calculated molecular weight of 23.8 kDa and a predicted pI value of 4.63. Five amino acid sequence blocks (block 1, block 2, block 3, block 4 and block 5) were found in Cry1Cb3. Translation of cry1Fb7 revealed an ORF of 3525 bp with 39.12% G+C content and a protein with a calculated molecular weight of 133.2 kDa and a predicted pI value of 5.18. Cry1Fb7 had five amino acid sequence blocks (blocks 1, 2, 3, 4 and 5) and three domains (I, II and III), which consisted of 218 residues (Leu

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.

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
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