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R C Jennings

Publications and source records attributed to R C Jennings.

11 recordsLinked to original sources

Evidence for a structural role for chlorophyll in chlorophyll-protein complexes.

1. Chymotrypsin treatment of spinach chloroplast membranes does not change the electrophoretic mobility of either chlorophyll-protein complex 1 or 2. 2. The extraction of lipids with 80% acetone after treatment of the membranes with chymotrypsin reveals that the polypeptide components of both chlorophyll-protein complexes had been extensively digested. The extraction of carotenes with petroleum ether under the same conditions does not change the electrophoretic mobility of the chlorophyll-protein complexes. 3. Fluorescence polarisation studies of chlorophyll-protein complex 2 reveal that the chymotrypsin digestion of this complex does not result in changes of mutual orientation or distance apart of chlorophyll a, chlorophyll b or carotenoid. 4. Two polypeptide components have been detected after lipid extraction of electrophoretically purified chlorophyll-protein complexes 1 and 2. The SDS molecular weights are 24 000 and 27 000 for complex 2, and 68 000 and 64 000 for complex 1. 5. We conclude that chlorophyll performs an important structural function in both chlorophyll-protein complexes.

Chlorophyll

Partition zone penetration by chymotrypsin, and the localization of the chloroplast flavoprotein and photosystem II.

1. Chymotrypsin treatment of chloroplast membranes inactivates Photosystem II. The inactivation is higher when the activity is measured under low intensity actinic light, suggesting that primary photochemistry is preferentially inactivated. 2. Membrane stacking induced by Mg2+ protects Photosystem II against chymotrypsin inactivation. When the membranes are irreversible unstacked by brief treatment with trypsin, Mg2+ protection against chymotrypsin inactivation of Photosystem II is abolished. 3. The kinetics of inactivation by chymotrypsin of Photosystem II indicates that membrane stacking slows down, but does not prevent, the access of chymotrypsin to Photosystem II, which is mostly located within the partition zones. 4. It is concluded that a partition gap exists between stacked membranes of about 45 A, the size of the chymotrypsin molecule. 5. The kinetics of inhibition of the chloroplast flavoprotein, ferredoxin-NADP reductase, bt its specific antibody is not affected by membrane stacking. This indicates that this enzyme is located outside the partition zones.

Chloroplasts

Studies on the slow fluorescence decline in isolated chloroplasts.

Data presented here indicate that the slow fluorescence decline in osmotically disrupted chloroplasts is not associated with the well known divalent cation effect on fluorescence yield. Thus the two phenomena have markedly different magnesium concentration requirements, magnesium addition after the fluorescence decline did not stimulate the dark reversal, and the characteristics of the fluorescence induction kinetics of the two processes are not similar. At pH 7.6 the slow fluorescence decline was stimulated by several uncouplers demonstrated to greatly reduce proton pumping, and at pH 9.2 it was stimulated by all uncouplers tested. Acid-base transition was strongly inhibitory, and this inhibition was relieved by coupling factor is suggested by experiments in which phosphorylation substrates were inhibitory, and this inhibition was prevented by uncoupler. These data are explained in terms of coupling factor structural changes which in an unknown manner influence Photosystem II fluorescence emission. Fluorescence induction curves indicate that the slow quenching decreased only the variable fluorescence. The half rise time was decreased along with the sigmoidicity of the rise curve. These data can be accomodated in terms of a model recently proposed by Butler and Kitajima (Biochim. Biophys Acta (1975) 376, 116-125), involving the transfer of energy from the excited, but closed, reaction centres II to the light harvesting chlorophyll system. The slow fluorescence decline is suggested to represent a decrease of this process.

Chlorophyll

Fluorescence induction in intact spinach chloroplasts.

Under conditions in which the Photosystem II quencher is rapidly reduced upon illumination, either after a preillumination or following treatment with dithionite, the fluorescence-induction curve of intact spinich chloroplasts (class I type) displays a pronounced dip. This dip is probably identical with that observed after prolonged anaerobic incubation of whole algal cells ("I-D dip"). It is inhibited by 3(3,4-dichlorophenyl)-1,1-dimethylurea and occurs in the presence of dithionite, sufficient to reduce the plastoquinone pool. It is influenced by far red light, methylviologen, anaerobiosis and uncouplers in a manner consistent with the interpretation that it represents a photochemical quenching of fluorescence by an electron transport component situated between the Photosystem II quencher and plastoquinone. Glutaraldehyde inhibition may indicate that protein structural changes are involved.

Anaerobiosis

Evidence for energy migration from photosystem I to photosystem II and the effect of magnesium.

1. With Euglena chloroplasts 7722 nm light excites a fluorescence induction pattern, measured at l,u nm, typical of the Photosystem II reduction of Q. 2. Both methylviologen and phenazine methosulfate partially quench this fluorescence rise in the absence of electron transport between Photosystem II and Photosystem I, and in a manner consistent with their known role of stimulating Photosystem I photochemistry. 3. The variable fluorescence excited with 22 nm light is reduced to a greater extent than that excited by 638 nm light upon chlorophyll dilution during division in the dark. 4. These observations are interpreted to indicate that in Euglena chloroplasts light absorbed by Photosystem I is transferred energetically "uphill" to Photosystem II, where it can perform Photosystem II photochemistry. 5. Magnesium ions stimulate the variable fluorescence with both 638 nm and 722 nm light to a similar extent, which argues against the concept of magnesium ion interrupting energy transfer between Photosystem II and Photosystem I.

Chlorophyll

Remission of active chronic hepatitis after treatment with cyclophosphamide and prednisolone. Report of four cases.

A description is given of four patients with active chronic hepatitis, all of whom were treated with prednisolone and cyclophosphamide. In all the patients diagnosis was established by the finding of a clinical picture of hepatic dysfunction associated with abnormal results of biochemical tests of liver function, evidence of disturbed immunity mechanisms and liver biopsy. After treatment all four patients made a clinical recovery. Three eventually had normal serum tests for liver function, normal bromsulphthalein excretion tests and normal histology in their needle liver biopsies. The fourth patient has shown considerable improvement in her serum tests of liver function, but she has been treated for a much shorter period than the others. Her test results are still improving. It is concluded that the combination of prednisolone and cyclophosphamide therapy is a satisfactory one for active chronic hepatitis, and probably superior to other therapeutic measures based upon the suppression of autoimmune mechanisms.

Adult