Catalase, bovine liver

Assay of photoprotein. The activity of the photoprotein was measured in 1ml of 20 mM Tris-HCl buffer, pH 8.0, containing 0.6 M NaCl at room temperature. The intensity and total amount of light emitted were recorded. The luminescence intensity is markedly intensified by adding 5 il of catalase solution (crystalline bovine liver catalase 1.5 mg/ml) and 10 pi of 3% H2O2. 

Abuchowski A, McCoy JR, Palczuk NC, van Es T, Davis FF (1977) Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J Biol Chem 252 3582-3586... 

DeMaster E.G., Dahlseid, T. and Redfern, B. (1994) Comparative oxidation of 2-propyn-l-ol with other low molecular weight unsaturated and saturated primary alcohols by bovine liver catalase in vitro. Chem. Res. Toxicol., 7 (3), 414-419. 

In another study, catalase derived from bovine liver was immobilized on the same polyurethane composite. The bovine liver catalase enzyme was obtained from City Chemical, West Haven, CT) and used without further purification. The activity of the enzyme was not stated or deteimined. 

Materials and Methods. Fully deuterated phycocyanin and protio phycocyanin from Ph. luridum were used. The method of purifying phycocyanin was identical to that used previously (15, 16). The purity of the phycocyanin preparations, the complete substitution of deuterium for hydrogen in the fully deuterated phycocyanin, and the reversibility of the aggregation phenomenon were ascertained as previously (4, 16). Purified bovine trypsin, soybean trypsin inhibitor, and bovine liver catalase were obtained from the Worthington Biochemical Corp., Freehold, N. J., and used without further purification. Bovine a -casein B was kindly supplied by Chien Ho of the University of Pittsburgh. 

Aside from the classical examples of hemoglobin and myoglobin, reaction of ferrous heme iron with O2 in hemeperoxidases has been reported for myeloperoxidase [60], horseradish peroxidase C [62], bovine liver catalase [68], lignin peroxidase [46], and lactoperoxidase [61]. With the exception of lactoperoxidase, the binding of O2 is irreversible and CIII engages in one or more of the decay pathways described below. 

Generation of CIII from GS occurs when the enzyme acts as an oxidase in the presence of superoxide ion. This reaction has been observed in horseradish peroxidase isoenzymes C and A2 [28, 53, 63], lignin peroxidase [46], myeloperoxidase [69], and bovine liver catalase [64], The rate constant for the reaction of GS with superoxide increases with a decrease of pH suggesting that the reacting species is HO2 instead of C - [64], The physiological relevance of the hydroxyperoxyl radical has been recently reassessed [70],... 

Lardinois OM (1995) Reactions of bovine liver catalase with superoxide radicals and hydrogen peroxide. Free Radic Res 22 251-274... 

Metodiewa D, Dunford HB (1992) Spectral studies of intermediate species formed in one-electron reactions of bovine liver catalase at room and low temperatures. A comparison with peroxidase reactions. Int J Rad Biol 62 543-553... 

Prakash K, Prajapati S, Ahmad A et al (2002) Unique oligomeric intermediates of bovine liver catalase. Protein Sci 11 46-57... 

Samejima T, Kamata M, Shibata K (1962) Dissociation of bovine liver catalase at low pH. J Biochem 51 181-187... 

Prajapati S, Bhakuni V, Babu KR et al (1998) Alkaline unfolding and salt-induced folding of bovine liver catalase at high pH. Eur J Biochem 255 178-184... 

Furuta H, Hachimori A, Ohta Y et al (1974) Dissociation of bovine liver catalase into subunits on acetylation. J Biochem 76 481 —491... 

Finally, the primary structure of bovine liver catalase (41), specifically between Gly-215 and Lys-220 (63a), is reminiscent of proximal histidine sequences, particularly in some cytochromes and globins (Table II) (41,... 

Fig. 11.10 Histogram of c7stallization hits for sparse matrix screens of model proteins. Number of screens tested on each protein are lysosyme (L)=2, glucose isomer-ase (Cl)=2, protease K (PK) = 1, bovine liver catalase (BLC) = 1, xylanase (X) = 2, bacterial primase catalytic core domain (BPC) = 3, bovine pancreas t7psin (BT) = 1, thaumatin (T) = l, mycobacterial RNase (MR)=3.

Yang L, Jia L, Zou H, and Zhang Y. Immobilized iminodiacetic acid (IDA)-t)fpe Cu chelating membrane affinity chromatography for purification of bovine liver catalase. Biomed. Chromatogr. 1999 13 229-234. 

Early ORD measurements on beef liver catalase showed large Cotton effects in the Soret region, which disappeared upon denaturation (255). No evidence for previously reported (256) Cotton effects near 600 nm could be obtained (255). ORD and CD measurements on bovine liver catalase included also the liganded hemoprotein. Conformational changes in the protein, occurring upon ligand addition, were deduced from data in the ultraviolet region (257). 

Betancor L, Hidalgo A, Femandez-Lorente G et al. (2003) Preparation of a stable biocatalyst of bovine liver catalase. Biotechnol Prog 19 763-767... 

Dextran cyclic imidocarbonate has been used to prepare soluble conjugates of a-amylase from Bacillus amyloliquefaciens and of bovine liver catalase for use in experimental enzyme therapy. The results suggest that by coupling the enzymes with a poorly antigenic macromolecule (dextran) anaphylactic reaction in animals pre-immunized with dextran may be suppressed or eliminated. Trypsin has been immobilized by reaction with dextran cyclic imidocarbonate. 

Human interferon-o2a, interleukin-2 receptor, human IgG, human serum albumin, dehydrogenases glucose-6-phosphate dehydrogenase, foanate dehydrogenase, pyruvate decarboxylase, S-oxynitrilase, bovine liver catalase, recombinant protein G, plasmid DMA, human blood coagulation factor VIII, enantiomers of kynurenine, tryptophan, beta-blockers, practolol, thic ntal... 

---