From beef liver

Acetoin dehydrogenase [from beef liver acetoin NAD oxidoreductase] [9028-49-3] Mr 76000, [EC 1.1.1.5]. Purified via the acetone cake then Ca-phosphate gel filtration (unabsorbed), lyophilised and then fractionated through a DEAE-22 cellulose column. The Km for diacetyl in 40pM and for... 

Acyl-coenzyme A Synthase [from beef liver] [9013-18-7] 57,000, [EC 6.2.1.2]. 

The molecular masses of heme catalases are usually significantly higher as compared with peroxidases. If expressed in Lg-1s-1, rate constants for the Fem-TAML activators when compared with catalase from beef liver, which has a molecular weight 250,000 gmol-1 (Table IV, entry 13) (89), look very impressive, viz. 17 L g 1 s-1 for 11 vs. 22 L g 1 s 1 for the enzyme. Nevertheless, the catalase-like activity of the Fem-TAML activators can be suppressed by the addition of electron donors -it is negligible in the presence of the substrates tested in this work. In Nature, catalases display only minor peroxidase-like activity (79) because electron donors bulkier than H202 cannot access the deeply buried active sites of these massive enzymes (90). The comparatively unprotected Fem-TAML active sites are directly exposed to electron donors such that the overall behavior is determined by the inherent relative reactivity of the substrates. 

J. G. N. De Jong, H. van den Bosch, D. Rijken, L. L. M. van Deenen, Studies on Ly-sophospholipases. III. The Complete Purification of Two Proteins with Lysophopho-lipase Activity from Beef Liver , Biochim. Biophys. Acta 1974, 369, 50-63. 

Cytoplasmic and mitochondrial aldehyde dehydrogenases (from beef liver) have also been inactivated by the hydrate 21 [21]. 

Kennedy, M. C., Mendemueller, L., Blondin, G. A., and Beinert, H. (1992). Purification and characterization of cytosolic aconitase from beef liver and its relationship to the iron-responsive element binding protein. Proc. Natl. Acad. Sci., USA 89, 11730. Knowles, R. G., Palacios, M., Palmer, R. M. j., and Moncada, S. (1989). Proc. Nad. Acad. 

Park, I. Ives, D.H. Kinetic mechanism and end-product regulation of deoxyguanosine kinase from beef liver mitochondria. J. Biochem., 117, 1058-1061 (1995)... 

Tomizawa HH. Properties of glutathione insulin trans-hydrogenase from beef liver. J Biol Chem 1962 237 3393-6. 

MULDOON M T and STANKER L H (1997), Molecularly imprinted solid phase extraction of atrazine from beef liver extracts , Anal Chem, 69, 803. 

The next major step was the development of an assay to determine the functional identity of the deduced PDesat-TnAllZ desaturase. Initial efforts to develop an in vitro reconstitutive biochemical assay combined the recombinant PDesat-TnAllZ protein purified from E. coli with phospholipids and a biochemical fraction from beef liver containing cytochrome b5 reductase and cytochrome b5. These efforts were unsuccessful (Knipple and Roelofs, unpublished). 

Kl. Kamp, H. H., Wirtz, K. W. A., and Van Deenen, L. L. M., Some properties of phosphatidylcholine exchange protein from beef liver. Biochim. Biophys. Acta 318,313-325 (1973). 

Note When preparations derived from beef liver are tested, the reaction is complete within 30 min. Preparations derived from Aspergillus and other sources may require up to 1 h. In assaying an enzyme of unknown origin, run a titration after 30 min and then at 10-min intervals thereafter. The reaction is complete when two consecutive titrations are the same. 

The synthesis of a-GalNAc derivatives has been achieved by an exoglycosidase a-iV-acetylgalactosaminidases from beef liver and Aspergillus. GalNAc-a-(l-0)-serine was prepared in 5% yield using GalNAca/>NP as the donor substrate and free serine as the acceptor (133). 

A preparation of heparin from beef liver was selected in 1942 by the Department of Biological Standards of the National Institute of Medical Research in London to serve as the provisional international standard. Quoted by (J.) E. Jorpes and S. Garden, Ref. 32. 

Cafalase from mosf eukaryotic species is tetra-meric. The protein from beef liver consists of 506-residue subrmifs. Human catalase is similar. ... 

The principle is based on an enzyme inhibition. Alkaline phosphatase (from beef liver) is inhibited by theophylline at a pH value of 8.2 (TRIS buffer). Endogenous alkaline phosphatase does not interfere, since its value of optimum is at a pH value of 10.5. 

The high affinity of Con A for cell surface oligosaccharides has also facilitated the immobilization of various cells including those of yeast [131], red blood cells [126, 128] and Trichosporon cutaneum [132]. An early study has also described the co-immobilization of enzymes and living cells using Con A [133]. More recently Habibi-Rezaei and Nemat-Gorgani [134] immobilized submitochondrial particles prepared from beef liver mitochondria on Con A support for continuous catalytic transformations involving succinate-cytochrome c reductase. 

Catalase (H202 H202 oxidoreductase EC 1.11.1.6) was one of the first enzymes to be isolated in a high state of purity, and its crystallization (29) from beef liver extracts ranked among the early triumphs of biochemistry. Extensive physicochemical studies which followed (30-41) led to an impressive elucidation of its properties, but as yet not to a definition of the apoprotein function in the enzyme catalysis. 

Huang, L.C., Heimark, D., Linko, J., Nolan, R., and Larner, J. A model phosphatase 2C->phosphatase 1 activation cascade via dual control of inhibitor-1 (INH-1) and DARPP-32 dephosphorylation by two inositol glycan putative insulin mediators from beef liver. Biochem. Biophys. Res. Commun., 1999, 255, 150-156. 

The effect of different phospholipid head groups on the protein-stimulated transfer by phosphatidylcholine- and phosphatidylinositol-specific proteins has been studied. Contradictory results were obtained for the effect of acidic phospholipids on the transfer of phospholipid by the phosphatidylcholine exchange protein from beef liver. DiCorleto et al. (1977) used small unilamellar vesicle-mitochondria and small unilamellar vesicle-multilamellar vesicles to study the effect of varying amounts of acidic phospholipids incorporated into phosphatidylcholine donor vesicles. Up to 20 mol% phosphatidic acid or phosphatidylinositol in the donor was found to stimulate the transfer of phosphatidylcholine in both assay systems. Wirtz et al. (1979) and Hellings et al. (1974) found different results for the phosphatidylcholine exchange protein with unilamellar and multilamellar vesicles. In these assays, the incorporation of acidic phospholipids (phosphatidic acid or phosphatidylinositol) into the donor particles had an inhibitory effect on the rate of phosphatidylcholine transfer. 

In other publications, Wallach et al.[66], Brooks et al.[731 and Kautz and Schnack-erz1401 gave detailed reports on the isolation and characterization of the dihydropyrimidinase from beef liver. Table 12.4-2 gives a short overview of the purification procedures and characteristic properties of these mammalian enzymes. The beef liver dihydropyrimidinase consists of four subunits and every active enzyme molecule contains four Zn(II)cations1731 which are tightly bound (Ks > 1.33 x 109 m 1). In addition to 5,6-dihydrouracil, glutarimide, thiohydantoin and barbituric acid are also accepted as substrates, but with low reaction rates1401. 

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