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F Addeo

Publications and source records attributed to F Addeo.

41 records · Page 3Linked to original sources
PubMed1976

[Primary structure of the casein macropeptide of caprine kappa casein].

The amino acid sequence of caprine CMP, the negatively charged C-terminal fragment released by chymosin (rennin EC 3.4.23.4) from goat K-casein at the initial stage of the milk-clotting process, has been investigated. The complete sequence has been determined by analysing chymotryptic and "thermolysin" fragments of the CMP. Caprine CMP contains 66 amino acid residues, 2 being phosphorylated. Asp2, Asn5, Thr11, Ser6, SerP2, Glu7, Gln2, Pro6, Ala9 Val5, Met1, Ile6, Lys3, His1, and the carbohydrate-free polypeptide chain has a molecular weight of 6,998 daltons. The occurrence in caprine CMP of an additional phosphate group, linked to serine 168 in the C-terminal region Thr-Ser168-Thr-Glu170-Val.OH of the polypeptide chain, has given support to the phosphorylation code for caseins that we postulated earlier [28, 27]. According to this hypothesis, a specific phosphoryl kinase may recognize an anionic phosphorylation site corresponding to the tripeptide sequence Thr/Ser-X-Glu, X being any amino acid residue. Since the C-terminal sequence of bovine and caprine CMPs differ by the substitution Ala/Glu170 (caprine), phosphorylation of caprine serine 168 could be explained by the occurrence of the new phosphorylation site Ser168-Thr-Glu170.

Amino Acid Sequence↗
PubMedDate not supplied

Primary structure of water buffalo beta-casein tryptic and CNBr peptides.

The partial amino acid sequence (70%) of water buffalo beta-casein has been determined by aligning the sequences of tryptic and CNBr peptides along the polypeptide chain of bovine beta-casein. Only five amino acid substitutions are observed. Moreover, as in all the beta-caseins so far investigated, a morphine-like peptide is present.

Amino Acid Sequence↗