Titlebook: Algal Development; Molecular and Cellul Wolfgang Wiessner,David G. Robinson,Richard C. Sta Conference proceedings 1987 Springer-Verlag Berl

擋泥板

Kinetic

Database and Expert Systems Applications2). The primary role of this protein has been deduced to be the site of binding of a plastoquinone molecule, Q. that functions in electron transport on the reducing side of PS-II; DCMU and atrazine compete at the Q. binding site. This interpretation is supported by the preferential labeling of a 32–

condone

聯(lián)邦

ablate

Interaction of Circadian Oscillators and the Cell Developmental Cycle in ,,t perturbations in phase? it would continue to function even if mitosis and division were blocked. Circadian oscillators (CO’s) may underlie the persisting circadian rhythms (CR’s) of cell division or of “hatching”, having longer periods of 20–28 h, frequently observed in populations of algae, fungi

提煉

archenemy

Comparison of Envelope Membranes From Higher Plants and Algae Plastids and of Outer Membranes From ere made possible owing to the development of efficient methods to purify large amounts of envelope membranes from higher plant chloroplasts. With the exception of ., few studies were done with algae plastid envelopes (Blee, 1981; Brandt, 1982/83), mostly due to the difficulty to prepare intact chlo

意見一致

Regulation of Chloroplast Differentiation: Cooperation between Light-Induced Processes and Internalrome b/f-complex (Cyt b/f) and the ATPase — composed of the intrinsic part CF. and the extrinsic part CF.. Approximately half of these proteins are encoded by the plastid chromosome, including all of the chlorophyll a-containing reaction center apoproteins and cytochrome, and half in the nucleus (He

能量守恒

,Evidence for Multiple Functions of the Intrinsic, 32–34 Kda Chloroplast Membrane Polypeptide of Sce2). The primary role of this protein has been deduced to be the site of binding of a plastoquinone molecule, Q. that functions in electron transport on the reducing side of PS-II; DCMU and atrazine compete at the Q. binding site. This interpretation is supported by the preferential labeling of a 32–

Arable

,“Life Cycle” of the 32 kDa-Protein of Chlamydomonas Chloroplasts,lated degradation. Under light stress conditions at 2000 μE/m./sec for 90 min the oxygen evolution declines and the 32 kDa-po1ypeptide is preferential1y synthesized . degraded at the same time (besides polypeptides of the RC II and LHC). During these stress conditions the specific radioactive labell