Results 261 to 270 of about 126,114 (304)

Reduction of renin-release by puromycin

Cardiovascular Research, 1970
Puromycin infused into a renal artery (10–125 μg/kg/min for 20 min) of anaesthetized dogs consistently reduced renin activity in samples of renal venous blood when kidneys were perfused at lowered pressures. It did not affect the smaller amounts of renin present in the renal venous effluent from kidneys perfused at normal pressures.
R D, Bunag, I H, Page, J W, McCubbin
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Synthesis of L,L‐Puromycin.

ChemInform, 2005
Abstract l , l -Puromycin, a diastereomer of the natural peptidyl nucleoside antibiotic puromycin, has been synthesized from l -xylose in 13 steps.
Carrie L.K. Gilbert, Christopher R. Lisek, Roger L. White, Giuseppe Gumina   +3 more
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Stereochemistry of the puromycin reaction

Biochemical and Biophysical Research Communications, 1971
Summary Space-filling models have shown that peptidyl-puromycin cannot be formed if puromycin is displacing the end of aminoacyl-tRNA. Instead, the models show that puromycin “hugs” the terminus of peptidyl-tRNA in such a way that the free amino group of the antibiotic is in a perfect position for a nucleophylic attack on the carbonyl carbon of the ...
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Inhibition of Interferon Action by Puromycin

The Journal of Immunology, 1965
Summary Puromycin, an inhibitor of protein synthesis, also inhibits the anti-viral action of interferon; this does not appear to be due to a block in the adsorption of interferon. The inhibition of interferon action is reversed by prolonged incubation of cells in buffer after removal of interferon and puromycin. When protein synthesis is
R M, Friedman, J A, Sonnabend
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Puromycin: Action on Neuronal Mitochondria

Science, 1968
Puromycin, in dosages that inhibit cerebral protein synthesis and expression of memory in mice, produces swelling of neuronal mitochondria. Acetoxycycloheximide, which inhibits cerebral protein synthesis to the same extent as puromycin, fails to produce swelling of neuronal mitochondria.
P, Gambetti, N K, Gonatas, L B, Flexner
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Puromycin analogs. Effect of aryl-substituted puromycin analogs on the ribosomal peptidyltransferase reaction

Journal of Medicinal Chemistry, 1981
A series of ortho- and para-substituted L-phenylalanylpuromycin analogues were synthesized and evaluated as substrates for the peptidyltransferase reaction of Escherichia coli ribosomes. Kinetic results reveal that substitution of the p-methoxy group of the puromycin molecule alters the peptidyltransferase activity of the molecule with the following ...
H, Lee, K L, Fong, R, Vince
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Structure of puromycin aminonucleoside

Acta Crystallographica Section C Crystal Structure Communications, 1988
3'-Amino-3'-deoxy-N,N-dimethyladenosine, $C_{12}H_{18}N_6O_3$, $M_r = 294.3$, monoclinic, $P2_1$, a = 4.684(1), b= 10.252(1), c= 14.381 (3)\AA, \beta = 91.16 (2)°, V= 690.49 $\AA^3$, Z = 2, $D_x = 1.39$ Mg $m^{-3}$, \lambda(Cu K\alpha) = 1.5418 \AA, \mu = 0.84 $mm^{-1}$, F(000) = 312, T= 295 K, R =0.045 for 986 observed reflections with I > 1.5\sigma(I)
Padmaja, N, Ramakumar, S, Viswamitra, MA
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Metabolism of puromycin by yeast cells

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1971
Abstract Yeast cells, supplied with high concentrations of puromycin, formed acyl aminoacyl puromycins and aminoacyl puromycins. These compounds were identified by their behaviour in chromatography and electrophoresis, by the incorporation of radioactive amino acids, acetate, and formate, and by reaction with 1-dimethylamino naphthalene-5-sulfonyl ...
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The Puromycin-Sensitive Aminopeptidase

2004
The puromycin-sensitive aminopeptidase (ApPS) was identified as the major enkephalin-degrading activity in brain, but has subsequently been implicated in a variety of cellular functions. In addition to regulating the concentration of neuropeptides, ApPS has been suggested to be involved in reproductive function, cell cycle regulation, regulation of ...
Michael W. Thompson, Louis B. Hersh
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Synthesis of a Puromycin Analog

Angewandte Chemie International Edition in English, 1968
F W, Lichtenhaler, H P, Albrecht
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