scholarly journals Terminal Amino Groups in Wool and S-Carboxymethyl Kerateine 2

1957 ◽  
Vol 10 (2) ◽  
pp. 225 ◽  
Author(s):  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Glutamic Acid ◽  
Aspartic Acid ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Total N ◽  
Purified Protein Derivative ◽  
Terminal Residue ◽  
Terminal Amino

The N-terminal residues of Merino 64's quality wool and of a purified protein derivative extracted from it, S-carboxymethyl kerateine 2, have been determined. A similar total N-terminal residue content is present in both wool and S�carboxymethyl kerateine 2 comprising glycine, serine, threoni~e, aspartic acid, glutamic acid, and alanine. These occur in different proportions in the two materials and valine is an additional N-terminal amino acid present only in wool.

scholarly journals Purification and Properties of Staphylocoagulase

1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Terminal Amino

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.

scholarly journals Carbohydrate is linked through ethanolamine to the C-terminal amino acid of Trypanosoma brucei variant surface glycoprotein

1983 ◽  
Vol 209 (1) ◽  
pp. 261-262 ◽  
Author(s):  
A A Holder
Keyword(s):  
Amino Acid ◽  
Aspartic Acid ◽  
Trypanosoma Brucei ◽  
Carboxy Group ◽  
Surface Glycoprotein ◽  
Variant Surface Glycoprotein ◽  
Side Chain ◽  
Serine Residue ◽  
Terminal Amino Acid ◽  
Terminal Amino

The C-terminal amino acid of the variant surface glycoprotein from Trypanosoma brucei is glycosylated. For two variant proteins that terminate in an aspartic acid and a serine residue respectively, it was shown that the sugar side chain is linked through ethanolamine to the alpha-carboxy group of the amino acid.

scholarly journals o-Quinones formed in plant extracts. Their reactions with amino acids and peptides

1969 ◽  
Vol 112 (5) ◽  
pp. 609-616 ◽  
Author(s):  
W. S. Pierpoint
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Plant Extracts ◽  
Thiol Group ◽  
Amino Group ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Secondary Reactions ◽  
Terminal Amino ◽  
Group 5

1. The reactions of amino acids and peptides with the o-quinones produced by the enzymic oxidation of chlorogenic acid and caffeic acid have been studied manometrically and spectrophotometrically. 2. Amino acids, except lysine and cysteine, react primarily through their α-amino groups to give red or brown products. These reactions, which compete with the polymerization of the quinones, are followed by secondary reactions that may absorb oxygen and give products with other colours. 3. The ∈-amino group of lysine reacts with the o-quinones in a similar way. The thiol group of cysteine reacts with the quinones, without absorbing oxygen, giving colourless products. 4. Peptides containing cysteine react with the o-quinones through their thiol group. 5. Other peptides, such as glycyl-leucine and leucylglycine, react primarily through their α-amino group and the overall reaction resembles that of the N-terminal amino acid except that it is quicker. 6. With some peptides, the secondary reactions differ from those that occur between the o-quinones and the N-terminal amino acids. The colours produced from carnosine resemble those produced from histidine rather than those from β-alanine, and the reactions of prolylalanine with o-quinones are more complex than those of proline.

scholarly journals Human complement component C4. Structural studies on the fragments derived from C4b by cleavage with C3b inactivator

1981 ◽  
Vol 199 (2) ◽  
pp. 351-357 ◽  
Author(s):  
E M Press ◽  
J Gagnon
Keyword(s):  
Amino Acid ◽  
Thiol Group ◽  
Peptide Bond ◽  
Carbohydrate Content ◽  
Amino Acid Sequences ◽  
Terminal Amino Acid ◽  
Radioactive Label ◽  
Terminal Residue ◽  
Alpha Chain ◽  
Terminal Amino

1. One of the activation products of C4, C4b, was prepared, and the reactive thiol group on the alpha′-chain was radioactively labelled with iodo[2-14C]acetic acid. The alpha′-chain was isolated and the N-terminal amino acid sequence of the first 13 residues was determined. 2. C4b was cleaved by C3bINA in the presence of C4b-binding protein and C4d and C4c isolated. The radioactive label and therefore the reactive thiol group were located to C4d. 3. C4c was reduced and alkylated and the two alpha′-chain fragments of C4c were separated. 3. The molecular weights, amino acid analyses and carbohydrate content of the three alpha′-chain fragments were determined. C4d has a mol.wt. of 44500 and a carbohydrate content of 6%. The two alpha′-chain fragments of C4c have mol.wts. of 25000 (alpha 3) and 12000 (alpha 4) and carbohydrate contents of 10 and 22% respectively. 4. The N-terminal amino acid sequences of C4d, the alpha 3 and the alpha 4 fragments were determined for 18, 24 and 11 residues respectively and, by comparison with the N-terminal sequence of the C4b alpha′-chain, the 25000-mol.wt. fragment (alpha 3) was shown to be derived from the N-terminal part of the alpha′-chain. 5. C-Terminal analyses were done on the alpha′-chain and its three fragments. Arginine was found to be the C-terminal residue of C4d and of the alpha 3 fragment. The C-terminal residue of the alpha′-chain and of the alpha 4 fragment could not be identified. The order of the three fragments of the alpha′-chain is therefore: alpha 3(25000)--C4d(44500)--alpha 4(12000). The specificity of C3bINA is for an Arg--Xaa peptide bond.

The Enzymic Digestion of Cod Tropomyosin

1962 ◽  
Vol 19 (6) ◽  
pp. 1095-1104
Author(s):  
B. Truscott ◽  
P. L. Hoogland ◽  
P. H. Odense ◽  
A. E. Waddell
Keyword(s):  
Amino Acid ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Performic Acid ◽  
Amino Acid Residues ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Enzymic Digestion ◽  
Disulphide Bonds ◽  
Terminal Amino

Tropomyosin from cod muscle can be oxidized with performic acid to cleave disulphide bonds without degradation of other amino acid residues. The ε-amino groups of lysine within the molecule can be substituted readily with carbobenzoxy-groups for protection against digestion by trypsin. The digestions by trypsin of carbobenzoxy-substituted tropomyosin, and by chymotrypsin of oxidized tropomyosin, have been shown to be reproducible, providing peptides suitable for amino acid sequence studies. The peptides so obtained were separated by ion-exchange chromatography using a Beckman/Spinco Amino Acid Analyzer.After treatment with urea, cod tropomyosin does not yield a free N-terminal amino acid as has been reported for rabbit tropomyosin.

Hog pancreatic α-amylase; N-terminal sequence analysis

1979 ◽  
Vol 44 (1) ◽  
pp. 145-147 ◽  
Author(s):  
Ivan Kluh
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Pancreatic Amylase ◽  
Terminal Sequence ◽  
Amino Groups ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Both isozymes of hog pancreatic amylase were digested with chymotrypsin, subtilisin and pronase. These digests were passed over a column of sulfoethyl-Sephadex C-25 and peptides not containing free NH2-groups thus isolated. It was shown that both isozymes have the same N-terminal amino acid sequence, pyrrolidonecarboxylic acid - tyrosine. No peptides with acetylated amino groups were found.

Immunoelectron microscope detection of C-type natriuretic peptide in normal human atrial tissue

1993 ◽  
Vol 51 ◽  
pp. 388-389
Author(s):  
Chi-Ming Wei ◽  
Margaret Hukee ◽  
Christopher G.A. McGregor ◽  
John C. Burnett
Keyword(s):  
Amino Acid ◽  
Natriuretic Peptide ◽  
Vascular Tone ◽  
Cardiac Tissue ◽  
Ring Structure ◽  
Terminal Amino Acid ◽  
Amino Acid Peptide ◽  
Normal Human ◽  
Terminal Amino ◽  
The Brain

C-type natriuretic peptide (CNP) is a newly identified peptide that is structurally related to atrial (ANP) and brain natriuretic peptide (BNP). CNP exists as a 22-amino acid peptide and like ANP and BNP has a 17-amino acid ring formed by a disulfide bond. Unlike these two previously identified cardiac peptides, CNP lacks the COOH-terminal amino acid extension from the ring structure. ANP, BNP and CNP decrease cardiac preload, but unlike ANP and BNP, CNP is not natriuretic. While ANP and BNP have been localized to the heart, recent investigations have failed to detect CNP mRNA in the myocardium although small concentrations of CNP are detectable in the porcine myocardium. While originally localized to the brain, recent investigations have localized CNP to endothelial cells consistent with a paracrine role for CNP in the control of vascular tone. While CNP has been detected in cardiac tissue by radioimmunoassay, no studies have demonstrated CNP localization in normal human heart by immunoelectron microscopy.

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