The Chemistry of Proteins and Peptides

Fraenkel‐Conrat, H.

doi:10.1146/annurev.bi.25.070156.001451

Cited by 23 publications

(6 citation statements)

References 124 publications

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“…WVhile there is no direct evidence that MC-leucylpeptides are present, the inference is strong and we conclude that the number of N-terminal leucine residues is more likely to be three, in agreement with Porter (1948), than two, as given by Fraenkel-Conrat (1956). All the fractions embraced in peak E gave an immediate reaction with ninhydrin and must therefore have contained peptides or free amino acids.…”

Section: Preparations Of Metholcycarbonylproteinssupporting

confidence: 75%

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Determination of the N-terminal residues in proteins with methoxycarbonyl chloride

Chibnall

Spahr

1958

Biochemical Journal

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Section: Preparations Of Metholcycarbonylproteinssupporting

confidence: 75%

“…5, Table 5) did not reveal any N-terminal residue, confirming earlier work in which FDNB had been used (cf. Fraenkel-Conrat, 1956).…”

Section: Peakmentioning

confidence: 99%

Determination of the N-terminal residues in proteins with methoxycarbonyl chloride

Chibnall

Spahr

1958

Biochemical Journal

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“…Peptides CH-3 and CH-5 lack lysine (Fig. 5), the amino acid predominantly acetylated by acetic anhydride at neutral pH, although hydroxyls in serine and, to a slight extent, tyrosine are occasionally attacked (Fraenkel-Conrat, 1962). Despite the low level of radioactivity in CH-3, 3H-acetylated glycophorin was frequently used in the present studies since, when combined with u.v.…”

Section: Separation Of Glycophorin Chymotryptic Peptides By Gel Filtrmentioning

confidence: 99%

A Sialoglycopeptide from Human Erythrocytes with Receptor-like Properties for Encephalomyocarditis and Influenza Viruses

Burness

Pardoe

1983

Journal of General Virology

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SUMMARYEncephalomyocarditis and influenza viruses attach to human erythrocytes causing haemagglutination. The receptor for both viruses on these cells is the major membrane sialoglycoprotein, glycophorin, solubilized preparations of which inhibit haemagglutination by either virus. We show here that glycophorin preparations inhibited haemagglutination of both viruses, even after the preparations were digested with chymotrypsin. To determine which component(s) in the digest exhibited activity, peptides separated by gel filtration were assayed for haemagglutination inhibition; one peptide only, CH-0, was active. A tentative structure was deduced for CH-0 from amino acid and sialic acid analyses. It was already known that neuraminidase treatment of erythrocytes or glycophorin prevents interaction with either virus, suggesting that sialic acid may form part of the active binding site in the receptor. However, receptor activity requires more than the presence of a particular arrangement of sialic acid since the arrangement in CH-0 was identical to that in two other inactive chymotryptic peptides. Examination by gel filtration, sucrose density gradient centrifugation and SDS-polyacrylamide gel electrophoresis demonstrated that CH-0 readily aggregated, unlike the inactive peptides. It was proposed that the CH-0 chymotryptic peptide showed receptor-like activity (inhibited haemagglutination) because its tendency to aggregate allowed strong multivalent binding with virus particles.

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“…Since no free NH2terminal residues for chain B and C were found we believe that they are blocked. In 1956, Fraenkel-Conrat and Singer [39] reported one NH,-terminal serine residue for their water-soluble dinitrophenyl derivative of crotoxin.…”

Section: Fractionation Of Reduced and Carboxamidomethylated Crotapotinmentioning

confidence: 99%

Biochemistry and Pharmacology of the Crotoxin Complex

Breithaupt

Rübsamen

Habermann

1974

European Journal of Biochemistry

102

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Crotapotin and the basic crotalus phospholipase A, which are the main components of the crotoxin complex, have been purified to homogeneity with respect to their behaviour on polyacrylamide gel electrophoresis, cellogel electrophoresis, immunoelectrophoresis, isoelectric focusing, and sedimentation equilibrium analysis.The isoelectric points were found to be 3.4 for crotapotin and 9.7 for the crotalus phospholipase A. The molecular weight of phospholipase A has been determined by gel filtration in 6 M guanidine . HCl (14 500), by ultracentrifugation (15 SOO), and by dodecylsulfate-gel electrophoresis (15 800). Phospholipase A consists of a single peptide chain intramolecularly crosslinked by eight disulfide bridges.The molecular weight of crotapotin was 8900 as shown by gel filtration in 6 M guanidine . HCl. Sedimentation equilibrium studies in 4 M guanidine . HCl gave a value of 6700. In solutions of lower ionic strength, the MI was 12 500, indicating that crotapotin can exist as a dimer. In contrast the M , of reduced and carboxamidomethylated crotapotin was much lower (4000 -4500), in gel filtration experiments.Crotapotin consists of three peptide chains, held together by disulfide bridges. Chain A contains 40 amino acid residues (MI 4274), chain B 34 residues (MI 3658) and chain C 14 residues (MI 1558). A free NH,-terminal residue (serine) could be detected only for chain A.The main toxic compound of the Crotalus terrificus venom, crotoxin, can be separated by chromatography on cilrboxymethyl cellulose into two basic phospholipases A with low toxicity, and the acidic crotapotin as reported by Habermann and Riibsamen [l], Breithaupt et al. [2] and Rubsamen et al. [3]. confirmed our results concerning the fractionation and recombination of the crotoxin complex. The acidic protein, which we have called crotapotin, lacks the toxicity and the enzymatic activity of crotoxin, but potentiates the toxicity and inhibits the enzymatic activities of the crotalus phospholipase A. The potentiating of the toxicity of phospholipase A was thought to be due to alteredThe previous two, papers in this series have appeared elsewhere [3,5]. A short outline of this paper was presented

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The Chemistry of Proteins and Peptides

Cited by 23 publications

References 124 publications

Determination of the N-terminal residues in proteins with methoxycarbonyl chloride

Determination of the N-terminal residues in proteins with methoxycarbonyl chloride

A Sialoglycopeptide from Human Erythrocytes with Receptor-like Properties for Encephalomyocarditis and Influenza Viruses

Biochemistry and Pharmacology of the Crotoxin Complex

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