Zobrazeno 1 - 10
of 141
pro vyhledávání: '"Jerome A. Schiff"'
Publikováno v:
Journal of General Microbiology. 139:251-257
Summary: Dark-grown resting (non-dividing) cells of Euglena gracilis var. bacillaris and mutants W3BUL (with a proplastid remnant) and W10BSmL (lacking plastids) incubated with 35SO2- 4 form a series of labelled lipids which are low or absent in divi
Publikováno v:
Journal of Structural Biology. 109:97-108
Cells of Euglena gracilis var. bacillaris or Z strain grown under the usual conditions (“nonwax cells”) and exposed to low-intensity light at the developmental threshold (3–7 ft-c) fail to accumulate LHCP II apoprotein. However, cells grown in
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1078:68-76
Two forms of ATP sulfurylase have been purified to homogeneity from mitochondria (ATPSm) and cells (ATPSc) of Euglena gracilis Klebs var. bacillaris Cori (aplastidic mutant W 10BSmL). Both forms are monomeric, ATPSc is 52.3 kDa and ATPSm is 55 kDa. T
Publikováno v:
Experimental Cell Research. 193:320-330
We have localized LHCP II apoprotein in the Golgi and thylakoids of Euglena gracilis Klebs var. bacillaris Cori and strain Z Pringsheim by electron microscopy using a specific antibody and protein A-gold. Using synchronized cells (light, 14 h:dark, 1
Autor:
Jerome A. Schiff, Jiayang Li
Publikováno v:
Biochemical Journal. 274:355-360
Adenosine 5′-phosphosulphate sulphotransferase (APSST) was extracted from Euglena gracilis Klebs var. bacillaris mutant W10BSmL by freezing and thawing and was purified about 10,000-fold (to homogeneity) with 10.5% recovery by (NH4)2SO4 precipitati
Autor:
Jerome A. Schiff
Publikováno v:
Ciba Foundation Symposium 72-Sulphur in Biology
Assimilatory sulphate reduction, largely restricted to plants and microorganisms where it provides reduced sulphur for the formation of amino acids and proteins, nucleic acids, and various sulphur-containing coenzymes, begins with the activation of s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06b497003f128270bc4f71a5afafcb8b
https://doi.org/10.1002/9780470720554.ch4
https://doi.org/10.1002/9780470720554.ch4
Publikováno v:
Cell Structure and Function. 15:99-105
Purification and properties of a phenol sulphotransferase from Euglena using L-tyrosine as substrate
Autor:
Jerome A. Schiff, Tekchand Saidha
A purification procedure based on (NH4)2SO4 precipitation, and chromatography on Affi-Gel Blue, DEAE-cellulose, hydroxyapatite and Bio-Gel P-60 yields a stable 6400-fold-purified active monomeric phenol (tyrosine) sulphotransferase of 26 kDa from W10
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f38c5dac27b9522d599b194121d9b1f
https://europepmc.org/articles/PMC1137981/
https://europepmc.org/articles/PMC1137981/
Autor:
Jerome A. Schiff, Jiayang Li
Publikováno v:
Plant and Cell Physiology.
Publikováno v:
Regulation of Chloroplast Biogenesis ISBN: 9781461364856
When dark-grown resting cells of Euglena are exposed to light at the low intensity threshold of chloroplast development(7 ft-c) the antennas, including the LHCP II 26.5 kD apoprotein are very low or undetectable, but on exposure of these cells to mor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::83cdb813f62c433c3808b6e8766d3c69
https://doi.org/10.1007/978-1-4615-3366-5_50
https://doi.org/10.1007/978-1-4615-3366-5_50