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pro vyhledávání: '"Mark D. Ball"'
Autor:
Chao-Hung Lee, Dhammika N. P. Nanayakkara, Pamela J. Durant, Marilyn S. Bartlett, Margaret M. Shaw, James W. Smith, Luiza R. S. Dias, James D. McChesney, Mark D. Ball
Publikováno v:
The Journal of eukaryotic microbiology. 44(6)
Publikováno v:
Biochemistry and cell biology = Biochimie et biologie cellulaire. 70(9)
The fatty-acid composition of retinyl esters in the livers of two species of phocid seal, the harp seal (Phoca groenlandica, n = 20) and the hooded seal (Cystophora cristata, n = 15), and one species of otariid seal, the California sea lion (Zalophus
Autor:
Mark D. Ball
Publisher Summary One of the reactions whereby retinol is esterified for storage in the liver is acyl-CoA-dependent transacylation, catalyzed by the microsomal enzyme acyl-CoA:retinol O-acyltransferase (ARAT). ARAT transfers the acyl group directly f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b66b6fbd34b8045259b55e849197eea
https://doi.org/10.1016/0076-6879(90)89321-8
https://doi.org/10.1016/0076-6879(90)89321-8
Publikováno v:
Journal of Inorganic Biochemistry. 43:330
Publikováno v:
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry. 84:513-517
1. 1. Acyl coenzyme A: retinol acyltransferase activity was identified in the microsomes from a polar bear liver. 2. 2. The highest rate of in vitro retinol esterification was 821 pmol/min/mg microsomal protein. 3. 3. The in vitro esterification rate
Publikováno v:
Biochemical and biophysical research communications. 128(1)
Retinol esterification by microsomal acyl coenzyme A:retinol acyltransferase was quantified in rat mammary tumor and liver tissue. Acyltransferase activity in the livers of mammary tumor-bearing rats was 40% of that in normal animals. In response to
Autor:
Mark D. Ball, James Allen Olson
Publikováno v:
Biochimica et biophysica acta. 961(1)
13-cis-Retinoic acid, a drug used at high doses in the treatment of recalcitrant acne, increased the permeability of rat-liver microsomal membranes to mannose 6-phosphate in vitro, as indicated by an increase in mannose-6-phosphatase activity. At the