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At least 469 records · Page 26Linked to original sources
PubMed2000

Identification of a phosphatase activity, toward the phosphopeptide pyroGlu-Asp-Asp-Ser(p)-Asp-Glu-Glu-Asn, in nuclear extract from HL-60 promyelocitic leukaemia cells.

Total protein extract from HL-60 cells was found to be able to dephosphorylate the RNA polymerase II octapeptide pyroGlu-Asp-Asp-Ser-Asp-Glu-Glu-Asn previously phosphorylated with protein kinase CKII (pCKII). Fractionation in cytoplasm, nuclear and chromatin extracts shows the phosphatase activity to be localized only in the nucleus, but not to be bound to the chromatin.

Casein Kinase II↗
PubMed2003

[Effect of casein phosphopeptides on bioavailability of the alimentary minerals].

Caseinophosphopeptides (CPPs) are phosphorylated casein-derived peptides which possess the ability to bind and solubilise minerals, such as Ca2+. The high bioavailability of Ca2+ fram milk and dairy products has been attributed to the production of CPPs which are produced following digestion of casein by the action of gastrointestinal proteinases. CPPs, which appear to be resistant to extensive proteolytic degradation, accumulate in the distal small intestine where they are purported to play a role in enhancing the passive absorption of Ca2+ and other trace elements. A recent human feeding tral reported improved Ca2+ and Zn2+ absorption following CPPs incorporation into food. This review summarises the production, characterization and potential applications of CPPs.

Biological Availability↗
PubMed1991

Amino acid analysis of proteins and tightly bound phosphopeptides in calf thymus DNA: indications of a novel regulatory mechanism.

Purification of DNA prepared from calf thymus nuclei, which were isolated at temperatures of -10 degrees to -15 degrees C, termed N-DNA, reduced the protein content from 17% to 0.7%. Amino acid analysis of the crude N-DNA revealed that the protein material removed in this process contained lys and phe, whereas in purified N-DNA neither of these amino acids was present. The crude N-DNA had a lower total Pser molar ratio (5.9) than that of the purified N-DNA (22.6). The purification also effected a large decrease of molecular weight, from 170 to 15 million daltons, roughly corresponding to the size of replicons. The amino acid composition of the N-DNA was compared with those of the two PP fractions, a) the PPs released into the dialysates, and b) the core material bound in the DNA, probably covalently, after reaction of N-DNA with EDTA and subsequent dialysis. N-DNA had an intermediate total Pser molar ratio between that of a) (35.3) and b) (11.9). Analysis of a standard preparation of DNA (S-DNA), which involved initial rupture of nuclei in the presence of cytoplasmic components, gave elevated values of asp and glu, a total Pser average value of 8.7 before, and 9.0, after the purification, and again phe and lys in the crude DNA.

Amino Acids↗