Melanie S Abbott

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The biosynthesis of ribulose bisphosphate carboxylase (RUBISCO) provides a model system for studying the coordination of nuclear and organelle gene expression, since this abundantly transcribed and expressed chloroplast enzyme is composed of small (SS) and large subunits (LS) encoded by a nuclear multigene family and a single chloroplast gene, respectively.(More)
The distribution of the Calvin cycle enzyme ribulose-1,5-bisphosphate carboxylase (RbuP(2)Case; EC 4.1.1.39) was examined by using two immunological methods in tissues of Solemya velum, an Atlantic coast bivalve containing putative chemoautotrophic symbionts. Antibodies elicited by the purified large subunit of RbuP(2)Case from tobacco (Nicotiana tabacum)(More)
INTRODUCTION To date, there is a paucity of comparative analysis of manual therapeutic procedures for the treatment of pain in the same spinal region. This paper examines the cross correlation of force-time histories across three distinct strategies of force production for the same thoracic spine procedure. Secondary analysis includes examination of the(More)
An analog of ADP containing an azido group at the C-2 position of the purine ring has been synthesized and used as an affinity probe of the membrane-bound coupling factor 1 of spinach chloroplast thylakoid membranes. The 2-azido-ADP inhibited light-induced dark binding of ADP at the tight nucleotide binding site on the thylakoid membranes. The 2-azido-ADP(More)
The photoaffinity analog 2-azido-ADP (2-azidoadenosine 5'-diphosphate) was used as a probe of the spinach chloroplast ATP synthase. The analog acted as a substrate for photophosphorylation. Several observations suggested that 2-azido-ADP and ADP bound to the same class of tight nucleotide binding sites: (a) 2-azido-ADP competitively inhibited ADP tight(More)
The photoaffinity analog 2-azido-ADP has been used to investigate the high-affinity binding site(s) for ATP on the chloroplast thylakoid membrane. Photophosphorylation of 2-azido-ADP results in the rapid formation of 2-azido-ATP, which remains tightly bound to the membranes after extensive washing. The kinetic parameters of the tight binding of ATP and of(More)
This work clarifies certain aspects of proton conductivity estimates in the light compared to dark conditions for spinach chloroplast thylakoid membranes. A method is presented, with kinetic analysis to justify it, that permits the separation of the proton influx and efflux rate constants, the sum of which contributes to the measured apparent first-order(More)
Nucleotide-binding sites on the chloroplast coupling factor 1 (CF1) have been probed using two photoreactive ADP analogs: 2-azido-ADP (2-N3-ADP) and 2',3'-O-(4-benzoyl)benzoyl-ADP (Bz-ADP). Photolabeling of the isolated CF1 with 2-N3-ADP results in incorporation of the analog exclusively into the beta-subunit of the enzyme. The location of the(More)
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