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Proteins lactate dehydrogenase

Exposure of rats for 6 hours/day, 5 days/ week for 4 weeks to 15 ppm caused corneal lesions in some of the rats along with reductions in total serum protein, lactate dehydrogenase, and serum albumin. Rats exposed to... [Pg.494]

S Nema, K Avis. Freeze-thaw studies of a model protein, lactate dehydrogenase, in the presence of cryoprotectants. Journal of Parenteral Science and Technology 47 76-83, 1992. [Pg.163]

Jervis used porous silica coated with chemisorbed polyacrylhydrazide for immobilization of adenosine monophosphate (AMP) [117]. After periodate oxidation of its ribose residue the ligand was coupled to the carrier and used for isolation of lactate dehydrogenase from rabbit muscle. The specific capacity was 2 mg of protein/g adsorbent with a ligand content of 10 pmol/g, whereas recovery of enzymatic activity after elution was 85%. Hipwell et al. [118] found that for effective binding of lactate dehydrogenases on AMP-o-aminoalkyl-Sepharose the spacer arm length required at least 4 methylene links. Apparently, a macromolecule of polyacrylhydrazide acts itself like an extended spacer arm and thus allow AMP to bind the enzyme. [Pg.169]

The shift in pattern of protein synthesis during anaerobiosis has been observed in root tissue of many other plant species including rice, sorghum, barley, pea, and carrot (see Sachs Ho, 1986). In anaerobically treated barley aleurone cells, lactate dehydrogenase (LDH) activity increases (Hanson Jacobsen, 1984) as does enzyme activity and mRNA levels for ADH (Hanson, Jacobsen Zwar, 1984). [Pg.168]

Rat (Fischer-344) 4 hr Resp 200 M (increase in protein and lactate dehydrogenase in lavage fluid focal areas of perivascular edema proteinaceous material in the alveoli) Green et al. 1991... [Pg.38]

Suaud-Chagny and Gonon [3] presented a new procedure for protein immobilization adapted to carbon microelectrode characteristics. The principle of this method of immobilization is based on the association of the protein with an inert porous film immobilized around the active tip of the electrode. For this purpose the carbon was coated with an inert, electrochemically obtained protein sheath (bovine serum albumin, BSA) a few micrometers thick. Then the sheath around the fiber was impregnated with lactate dehydrogenase (LDH), which could be immobilized onto the electrode and resulted in an electrode sensitive to pyruvate. [Pg.556]

Table 1.7 Activity of lactate dehydrogenase after freezing and thawing in the presence of dissolved substances, which are mostly repelled by proteins (Table III from [1.18]). Table 1.7 Activity of lactate dehydrogenase after freezing and thawing in the presence of dissolved substances, which are mostly repelled by proteins (Table III from [1.18]).
Figure 8.10 The quaternary structure of proteins. The enzyme lactate dehydrogenase (EC 1.1.1.27) has a relative molecular mass of approximately 140 000 and occurs as a tetramer produced by the association of two different globular proteins (A and B), a characteristic that results in five different hybrid forms of the active enzyme. The A and B peptides are enzymically inactive and are often indicated by M (muscle) and H (heart). The A4 tetramer predominates in skeletal muscle while the B4 form predominates in heart muscle but all tissues show most types in varying amounts. Figure 8.10 The quaternary structure of proteins. The enzyme lactate dehydrogenase (EC 1.1.1.27) has a relative molecular mass of approximately 140 000 and occurs as a tetramer produced by the association of two different globular proteins (A and B), a characteristic that results in five different hybrid forms of the active enzyme. The A and B peptides are enzymically inactive and are often indicated by M (muscle) and H (heart). The A4 tetramer predominates in skeletal muscle while the B4 form predominates in heart muscle but all tissues show most types in varying amounts.
E. Miscellaneous antiparallel /3 Gene 5 protein, E. coli Lactate dehydrogenase domain 2 Tomato bushy stunt virus protein domain 1 IV. Small disulfide-rich or metal-rich domains... [Pg.259]

The doubly wound structures were first recognized as a category by Rossmann in comparing flavodoxin with lactate dehydrogenase dl. As more and more protein structures were solved which fell into this... [Pg.290]

The remaining three antiparallel /3 structures form a miscellaneous category (see Fig. 84). Lactate dehydrogenase d2 and gene 5 protein each has several two-stranded antiparallel j8 ribbons, but they do not coalesce into any readily described overall pattern. The N-terminal domain of tomato bushy stunt virus protein has a unique /3 structure in which equivalent pieces of chain from three different subunits wrap around a 3-fold axis to form what has been called a /3 annulus (Harrison et ah, 1978). Each of the three chains contributes a short strand segment to each of three three-stranded, interlocking /3 sheets. This domain provides one of the subunit contacts that hold the virus... [Pg.305]


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See also in sourсe #XX -- [ Pg.664 , Pg.665 , Pg.700 ]




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