Zobrazeno 1 - 10
of 17
pro vyhledávání: '"E L Triplett"'
Publikováno v:
DNA and Cell Biology. 15:605-616
Phosvitins are extensively phosphorylated serine-rich proteins that are derived from a large hepatic phosphoglycolipoprotein, vitellogenin, and are deposited, after suitable processing, in the eggs of oviparous vertebrates. Despite their widespread o
Autor:
Barbara B. Prézelin, Roberto Iglesias-Prieto, Robert K. Trench, S. J. Roman, Nadathur S. Govind, E. L. Triplett
Publikováno v:
Proceedings of the Royal Society of London. B. Biological Sciences. 240:187-195
Affinity-purified antibodies prepared against the peridinin-chlorophyll a -protein (PCP) complex from the dinoflagellate Heterocapsa pygmaea were employed to study the immunological similarity of PCP among 28 dinoflagellate species, representing eigh
Publikováno v:
Journal of protein chemistry. 15(1)
Phosvitins are the principal phosphoproteins in the eggs of oviparous vertebrates. They have an exceptionally high serine content and most, or even all, of the serine residues are esterified to phosphate. The phosphorylated residues tend to occur in
Publikováno v:
Molecular marine biology and biotechnology. 2(4)
Characterizations are presented for RNA, 2 cDNA libraries, and 2 full-length cDNA sequences encoding for photosynthetic light-harvesting peridinin-chlorophyll a-protein (PCP) in the dinoflagellate Heterocapsa pygmaea. Subsequent analyses of the PCP s
Autor:
E L Triplett, C Wittenberg
Publikováno v:
Journal of Biological Chemistry. 260:12542-12546
Tyrosinase purified from Xenopus is enzymatically inactive in aqueous buffers but is activated for both of its substrates by exposure to a variety of anionic detergents. Cationic and nonionic detergents, as well as a variety of other agents are ineff
Autor:
E L Triplett, Glen N. Gaulton
Publikováno v:
Journal of Biological Chemistry. 258:14845-14849
The relationship between the process of neural induction and the control of tyrosinase gene expression in the cells that derive from the neural crest of amphibians has been examined at the molecular level. [3H] Tyrosinase cDNA was utilized as a probe
Autor:
C Wittenberg, E L Triplett
Publikováno v:
Journal of Biological Chemistry. 260:12535-12541
A tyrosinase has been purified from the skin of the frog Xenopus laevis. Dihydroxyphenylalanine oxidase and tyrosine hydroxylase activities co-purify throughout the procedure. The enzyme is isolated in an inactive form, but both enzymatic activities
Autor:
R B Mikkelsen, E L Triplett
Publikováno v:
Journal of Biological Chemistry. 250:638-643
Two enzymes with tyrosinase activity have been purified from the frog Rana pipiens. Both enzymes are isolated in an inactive form which can be activated with trypsin. Amino acid analysis, NH2-terminal amino acid determination (arginine for both prote
Autor:
E L Triplett, Glen N. Gaulton
Publikováno v:
Journal of Biological Chemistry. 258:14839-14844
Rana pipiens tyrosinase mRNA was isolated from Stage 22 (tailfin circulation) embryos by indirect immunoprecipitation of embryonic polysomes using highly specific rabbit anti-tyrosinase and goat-(anti-rabbit) immunoglobulins. Analysis on sucrose grad
Publikováno v:
Development. 24:109-118
A population of polysomes isolated from frog skin is capable of supporting protein synthesis in a cell-free system containing an energy generating system, ‘soluble components and amino acids. These polysomes catalyse the oxidation of DOPA after gen