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At least 397 records · Page 22Linked to original sources
PubMed1987

Structural studies on neonatal rat liver glycogen synthase: a comparison between adult and newborn synthase phosphopeptides.

Liver glycogen synthase has been isolated from newborn rats and phosphorylated in vitro with the catalytic subunit of cAMP-dependent protein kinase. The isolated newborn synthase b is dependent upon Glc 6-P for activity, like adult synthase b, but has a high affinity toward Glc 6-P, unlike adult synthase b but like adult synthase a. Phosphorylation decreases the newborn synthase affinity toward Glc 6-P to the same value as adult synthase b. A comparison of adult and newborn synthase 32Pi-labeled trypsin and chymotrypsin peptide fragments by sodium dodecyl sulfate-polyacrylamide gel electrophoresis shows that the newborn synthase has structural properties significantly different from the adult enzyme. Thus, a fetal isozyme of synthase in the newborn rat could account, in part, for the difference in catalytic properties, relative to adult synthase.

Aging↗
PubMed1976

A kinetic analysis of the dephosphorylation, by bovine spleen phosphoprotein phosphatase (EC 3.1.3.16) of a phosphopeptide derived from beta-casein.

A peptide containing the four closely grouped phosphoseryl residues present in beta-casein has been enzymatically dephosphorylated with bovine spleen phosphoprotein phosphatase (EC 3.1.3.16). The course of the dephosphorylation reaction has been followed by cellulose acetate electrophoresis and the amount of partially phosphorylated peptides present at each stage quantified by the same method. The phosphate groups are shown to be removed in a sequential manner and the rate constants for each stage of the dephosphorylation have been computed from the data obtained. The rate constants indicate that interaction in the intact peptide results in an enhancement of the activity of the phosphoseryl cluster.

Caseins↗
PubMed1990

Phosphorylation of src-phosphopeptides by casein kinases-1 and -2: favourable effect of phosphotyrosine.

The synthetic phosphotyrosyl tridecapeptide H-Arg-Leu-Ile-Glu-Asp-Asn-Glu-Tyr(P)-Thr-Ala-Arg-Gln-Gly-OH, reproducing a major phosphoacceptor site of protein tyrosine kinases of the src-family, can be phosphorylated at Thr-9 by both casein kinases -1 and -2. Its shorter derivative H-Asn-Glu-Tyr(P)-Thr-Ala-OH is not affected by casein kinase-1 while representing a substrate as good as the tridecapeptide for casein kinase-2. The unphosphorylated analogue H-Asn-Glu-Tyr-Thr-Ala-OH, however, is a much poorer substrate, and no significant phosphorylation could be observed of its O-methyl ether derivative H-Asn-Glu-Tyr(Me)-Thr-Ala-OMe. These data on one side corroborate the concept that casein kinase-1 recognizes residues located on the C-terminal edge of acidic stretches, providing, on the other, the evidence that phosphotyrosyl side chains can act as specificity determinants for casein kinase-2.

Amino Acid Sequence↗
PubMed1995

Separation of phospho- and non-phosphopeptides using reverse phase column chromatography.

Peptides containing phosphoserine, phosphothreonine or phosphotyrosine and their parent non-phosphorylated forms were chromatographed using standard C18 reverse phase chromatography in the presence of a water/acetonitrile gradient supplemented with different counter ions. We obtained the best separation of phosphorylated from non-phosphorylated peptides in the presence of heptafluorobutyric acid, with differences in retention times as large as approximately 20 min. The chromatographic method was reliable in separation of the same peptides phosphorylated at different positions, acidic or basic phospho-Ser/Thr-peptides or phospho-Tyr-containing peptides. The described separation conditions are useful in studying the kinetics of phosphorylation/dephosphorylation and in analysis of phosphorylation sites in vivo.

Amino Acid Sequence↗
PubMed1991

Monovalent cation-dependent reversible phosphorylation of ribosomal protein S8 in growth arrested Tetrahymena: kinetics of formation, phosphoamino acids, and phosphopeptides of mono-, and diphosphorylated derivatives of protein S8.

The kinetics of formation of mono-, and diphosphorylated derivatives of ribosomal protein S8 in Tetrahymena starving in the presence of Na+ have been determined, and the phosphoamino acids present in these derivatives have been identified. The mono-phosphorylated product, S8', contains only phosphoserine, and behaves kinetically as the precursor of the diphosphorylated product S8" which contains phosphoserine, and phosphothreonine. Tryptic digestion release a single major phosphoserine containing peptide from both S8' and S8", and a single phosphothreonine containing peptide from S8".

Amino Acid Sequence↗
PubMed1986

Non-competitive inhibition of ornithine decarboxylase by a phosphopeptide and phosphoamino acids.

In Tetrahymena pyriformis the cytosolic ornithine decarboxylase (L-ornithine carboxy-lyase, EC 4.1.1.17) activity is considerably inhibited by the presence of polyamines in the growth medium, while the nuclear ornithine decarboxylase is only slightly affected. Experimental evidence suggests that the presence of putrescine and/or spermidine elicits the appearance of non-competitive inhibitors of ornithine decarboxylase. One of the inhibitors has a molecular weight of 25,000 and properties of antizyme. In addition, two other low molecular weight inhibitors are extracted, one which is a phosphoserine oligopeptide, and the other which is phosphotyrosine. All inhibit non-competitively the homologous and heterologous (Escherichia coli and rat liver) ornithine decarboxylases. Similarly, non-competitive inhibition was obtained when the commercially available phosphoamino acids were tested against the already mentioned ornithine decarboxylases.

Amino Acids↗