1986
DOI: 10.1093/oxfordjournals.jbchem.a121809
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Purification and Characterization of 3-Hydroxy-3-Methylglutaryl CoA Reductase from Potato Tubers

Abstract: 3-Hydroxy-3-methylglutaryl coenzyme A reductase (NADPH) was solubilized by trypsin digestion from sliced potato tuber microsomes, and purified to apparent homogeneity in the absence of detergent with a recovery of 1.8%. The enzyme had a specific activity of 7,910 nmol of mevalonate formed per min per mg of protein. On molecular-sieving high-performance liquid chromatography, the activity was coincident with the single protein peak corresponding to a molecular weight of approximately 110 kDa. On SDS-polyacrylam… Show more

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Cited by 16 publications
(9 citation statements)
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“…7 pM and that for (S)-HMGCoA was 8.3 2 1 .5 pM. Table 2 shows the apparent K,,, values of the HMGRlcd for both substrates compared with those obtained in previous studies performed either with purified HMGR from radi5h [35], potato [45] and Hevea brasiliensis [44] or partially purified HMGR from maize [S].…”
Section: Resultsmentioning
confidence: 96%
“…7 pM and that for (S)-HMGCoA was 8.3 2 1 .5 pM. Table 2 shows the apparent K,,, values of the HMGRlcd for both substrates compared with those obtained in previous studies performed either with purified HMGR from radi5h [35], potato [45] and Hevea brasiliensis [44] or partially purified HMGR from maize [S].…”
Section: Resultsmentioning
confidence: 96%
“…(1985) suggest a transcriptional component to the induction of potato HMGR activity. The instability of HMGR enzymes (Kondo and Oba, 1986) precluded purification of the different isoforms and gene isolation by oligonucleotides derived from amino acid sequence information. Therefore, we determined whether a highly conserved C-termina1 region of an Arabidopsis HMGR cDNA (Learned and Fink, 1989) would hybridize with potato nuclear DNA.…”
Section: Lsolation and Sequence Analysis Of Potato Hmgr Cdnasmentioning
confidence: 99%
“…HMGR was solubilized from the microsomal fraction by using trypsin and puriˆed by a‹nity chromatography (2?,5?-ADP-Sepharose and HMG-CoA-HexaneAgarose) as described previously. 25) Preparation of polyclonal antibody against HMGR. Three male BALB W c mice received subcutaneous injection of 5-10 mg protein of puriˆed HMGR in 50 ml of 10 mM potassium phosphate buŠer (pH 7.5) emulsiˆed in an equal volume of complete Freund's adjuvant four times, i.e., on d 0,11, 21, and 45.…”
Section: )mentioning
confidence: 99%
“…This molecular mass is close to the size of the puriˆed HMGR from the microsomal fraction of cut potato tuber tissue as previously described. 25) This monoclonal antibody also recognized a single band with a molecular mass of 64.5 kDa corresponding to SDS-solubilized fraction from microsomal suspen- The puriˆed enzyme (ng) was incubated in wells previously coated with monoclonal antibody (mAb-5A5) and then the labeled probe, 125 I-labeled monoclonal antibody (mAb-1H5) was added. The radioimmunoassay in a well was assayed as described in the text.…”
Section: Characterization Of Monoclonal Antibodymentioning
confidence: 99%
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