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B Ribadeau Dumas

Publications and source records attributed to B Ribadeau Dumas.

11 recordsLinked to original sources
PubMed1985

Kinetics of the action of chymosin (rennin) on a peptide bond of bovine alpha s1-casein. Comparison of the behaviour of this substrate with that of beta- and kappa o-caseins.

The action of chymosin on the Phe23-Phe24 bond of bovine alpha s1-casein, in citrate buffer (pH 6.2) at 30 degrees C, was followed by reversed-phase HPLC quantification of residual alpha s1-casein or fragment 24-199 after different time periods and at different substrate concentrations. This allowed determination of the Michaelian parameters for the reaction under study which were compared with those previously obtained for the action of chymosin on beta- and kappa o-casein under identical reaction conditions. The whole efficiency of the three reactions, as estimated by kcat/Km, was 1.8, 20.6 and 1405.0 for alpha s1-, beta- and kappa o-caseins, respectively. The specificity of chymosin is discussed in the light of these results and of the known sequences of the 3 caseins.

Amino Acid Sequence↗
PubMed1982

Study of the heterogeneity of bovine pepsin A by pseudo isoelectric focusing.

Pseudo isoelectric focusing (PIEF), i.e. focusing stopped before the equilibrium is reached, has been successfully applied to analyse bovine pepsins A obtained from abomasum mucosa extracts and from 3 individual abomasal juices. Whole bovine pepsin A from mucosa extracts, was resolved in PIEF, using an acidic pH gradient(2-4), into five major and active components. Its fractionation on hydroxyapatite only gave four components which were not homogeneous in PIEF, suggesting that interactions between the different components occur during the chromatographic procedure. After treatment with potato acid phosphatase, whole bovine pepsin A showed only one band in PIEF, displaying enzymic activity and with a mobility identical to that of the less anodic band in untreated pepsin. These results, together with organic phosphate determinations, obviously confirm that the heterogeneity of bovine pepsin A is due to the phosphate content which appears to range between 0 and 3 mol./mol. for the 5 components. Two of them, the phosphate content of which appears to be 1 mol./mol., seem to differ in the location of this phosphate group in the molecule. Whole bovine pepsin A preparations from abomasal juices shared the same pattern in PIEF, identical to that observed with bovine pepsin A from mucosa extracts, thus excluding that dephosphorylation might be involved in the secretory process, as well as disproving the theory that dephosphopepsinogen might be an intermediate in the synthesis of pepsinogen, as it was previously suggested.

Abomasum↗
PubMed1976

[The primary structure of bovine alpha s2 caseins].

The bovine alphas2-, alphas3-, alphas4- and alphas6-caseins [1] were isolated. The 4 proteins had the same amino-acid composition and C-terminal sequence, but different phosphorus contents. From a mixture of these proteins (designated as 'alphas2-complex') and from alphas3-casein a single and identical N-terminal sequence was obtained by Edman degradation. It seems therefore that the 4 proteins have the same peptide chain and only differ in their phosphorus content. For this reason we propose to modify the nomenclature of Annan and Mason [1] and to use in future the single term alphas2 to designate the caseins which have been previously called alphas2,alphas3,alphas4 and alphas6 by these authors. The study of the primary structure of the peptide chain, which has confirmed these results, was undertaken on the S-carboxymethylated alphas2-complex. From a cyanogen bromide digest and from a tryptic hydrolyzate of the alphas2-complex, 5 and 25 peptides were obtained respectively, both sets of peptides accounting for the whole peptide chain. Examination of the tryptic peptides containing methionine combined with the N- and C-terminal sequences of the alphas2-complex and some CNBr peptides, gave the order of the CNBr peptides, H.CN4--CN2--CN5--CN1--CN3.OH, which contain 4, 22, 115, 49 and 17 residues respectively. A partial sequence accounting for half of the peptide chain of the alphas2-complex is given. This peptide chain is likely composed of 207 amino-acid residues.

Amino Acid Sequence↗