Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.14 (ATP synthase)
 7,042 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The ceroid-lipofuscinoses (Batten's disease) are a group of recessively inherited lysosomal storage diseases of children and animals in which there is intracellular accumulation of a fluorescent lipopigment in a wide variety of cells. Lipopigment bodies isolated from pancreas, liver, kidney and brain tissue from a heifer affected with ceroid-lipofuscinosis contained between 55 and 62% protein. A dominant component comigrated on LDS-PAGE with the major low molecular weight protein stored in ovine ceroid-lipofuscinosis. It was identified by amino acid sequence and mass spectroscopy as the full subunit c of mitochondrial ATP synthase, normally found only in the inner mitochondrial membrane, where it is estimated to account for 2-4% of the membrane protein. In pancreatic lipopigment it accounted for at least 40% of the total lipopigment mass and this storage was considered specific to the disease. No other mitochondrial proteins were found in storage bodies. These results are similar to those found in studies on the ovine and the late infantile and juvenile human forms of the disease. It is concluded that bovine ceroid-lipofuscinosis is also a proteolipid proteinosis in which subunit c of mitochondrial ATP synthase is specifically stored in lysosome derived organelles.
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PMID:Bovine ceroid-lipofuscinosis (Batten's disease): the major component stored is the DCCD-reactive proteolipid, subunit C, of mitochondrial ATP synthase. 182 67

A chlorophyll-protein complex has been isolated from the cyanobacterium Synechocystis sp. PCC 6803 that closely resembles higher plant photosystem II reaction centers in spectral properties. The Synechocystis complex has a pigment content of 5-7 chlorophyll a molecules:1 Cyt b559:2 pheophytins; an optical absorption redmost transition at approximately 675 nm; and a nonconservative circular dichroism red signal, with extrema at 682 (+) and 652 (-) nm. Upon illumination, the Synechocystis D1/D2/Cyt b559 complex accumulates reduced pheophytin. LDS-PAGE and/or immunoblotting showed the D1, D2, and Cyt b559 proteins, aggregated and degraded forms of D1 and possibly D2, and traces of ATP synthase and the CP47 photosystem II chlorophyll protein. The availability of such a Synechocystis preparation opens the way for employing site-directed mutagenesis in studying primary reactions of oxygenic photosynthesis.
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PMID:Isolation and spectroscopic characterization of a plantlike photosystem II reaction center from the cyanobacterium Synechocystis sp. 6803. 772 12