scholarly journals Neurodegeneration due to 3-hydroxyisobutyryl-CoA hydrolase deficiency

2020 ◽  
Author(s):  
Keyword(s):  
Coa Hydrolase

scholarly journals Capsicum anum L. Derived Phytochemicals against Haemophilus influenzae Causing Bronchitis

2020 ◽  
pp. 100-103
Author(s):  
Debadatta Nayak ◽  
Debesh Kumar Hota ◽  
Tophani Sahu ◽  
Soumya Jal ◽  
Dipankar Bhattacharyay
Keyword(s):  
Molecular Docking ◽  
Life Cycle ◽  
Haemophilus Influenzae ◽  
Interaction Energy ◽  
Plant Extract ◽  
Haemophilus Influenza ◽  
Discovery Studio ◽  
Docking Method ◽  
Coa Hydrolase ◽  
Molecular Docking Method

Phytochemicals from Capsicum anum L. plant extract are traditionally used to cure bronchitis. Bronchitis is caused by Haemophilus influenzae. Molecular docking method applied using “Biovia Discovery Studio”. “High positive values of -CDOCKER energy and -CDOCKER interaction energy” suggested that myrcetin and quercetin can effectively deactivate the Palmitoyl-CoA hydrolase enzyme thereby interrupting the life cycle of Haemophilus influenza.

Acetoacetyl-CoA hydrolase

1991 ◽  
pp. 261-263
Author(s):  
Dietmar Schomburg ◽  
Margit Salzmann
Keyword(s):  
Coa Hydrolase

scholarly journals Isolation of palmitoyl-CoA hydrolases from human blood platelets

1981 ◽  
Vol 199 (3) ◽  
pp. 639-647 ◽  
Author(s):  
R K Berge ◽  
L E Hagen ◽  
M Farstad
Keyword(s):  
Human Blood ◽  
Blood Platelets ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Apparent Molecular Weight ◽  
Cytosol Fraction ◽  
Molecular Weights ◽  
Apparent Homogeneity ◽  
Coa Hydrolase ◽  
Human Blood Platelets

The palmitoyl-CoA hydrolase activity, which in human blood platelets is mainly localized in the cytosol fraction [Berge, Vollset & Farstad (1980) Scand. J. Clin. Lab. Invest. 40, 271--279], was found to be extremely labile. Inclusion of glycerol or palmitoyl-CoA stabilized the activity during preparation. Gel-filtration studies revealed multiple forms of the enzyme with molecular weights corresponding to about 70 000, 40 000 and 24 000. The relative recovery of the mol.wt.-70 000 form was increased by the presence of 20% (v/v) glycerol or 10 microM-palmitoyl-CoA. The three enzyme forms are probably unrelated, since they were not interconvertible. The three different species of palmitoyl-CoA hydrolase were purified by DEAE-cellulose and hydroxyapatite chromatography, isoelectric focusing and high-pressure liquid chromatography (h.p.l.c.) to apparent homogeneity. The three enzymes had isoelectric points (pI) of 7.0, 6.1 and 4.9. The corresponding molecular weights were 27 000--33 000, 66 000--72 000 and 45 000--49 000, calculated from h.p.l.c. and Ultrogel AcA-44 chromatography. The apparently purified enzymes were unstable, as most of the activity was lost during purification. The enzyme with an apparent molecular weight of 45 000--49 000 was split into fractions with molecular weights of less than 10 000 by re-chromatography on h.p.l.c. concomitantly with a loss of activity. The stimulation of the activity by the presence of serum albumin seems to depend on the availability of palmitoyl-CoA, as has been reported for other palmitoyl-CoA hydrolases. [Berge & Farstad (1979) Eur. J. Biochem. 96, 393--401].

Influence of dietary status and diabetes on aortic acyl-CoA hydrolase activity

1977 ◽  
Vol 26 (3) ◽  
pp. 289-296 ◽  
Author(s):  
Sam Hashimoto ◽  
Seymour Dayton
Keyword(s):  
Hydrolase Activity ◽  
Coa Hydrolase
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