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Lysozome

Information concerning the effects of selenium in man is lacking and it is doubtful whether administration of selenium in man has any effect on the toxicity of mercuric mercury. However, mercury and selenium were found in the cellular lysozomes in renal tubular cells in two patients with inorganic mercury poisoning [143]. [Pg.199]

Rat Wistar 3 or 10 d ad lib (F) Endocr 2000 M (decreased T4 levels, damaged mitochondria, increased number and size of lysozomes, enlarged Golgi apparatus)... [Pg.28]

Cathepsin D (EC3.4.23.5). It has been known for more than 20 years that milk also contains an acid proteinase, (optimum pH ss 4.0) which is now known to be cathepsin D, a lysozomal enzyme. It is relatively heat labile (inactivated by 70°C x 10 min). Its activity in milk has not been studied extensively and its significance is unknown. At least some of the indigenous acid proteinase is incorporated into cheese curd its specificity on asl- and / -caseins is quite similar to that of chymosin but it has very poor milk-clotting activity (McSweeney, Fox and Olson, 1995). It may contribute to proteolysis in cheese but its activity is probably normally overshadowed by chymosin, which is present at a much higher level. [Pg.241]

Other proteinases. The presence of low levels of other proteolytic enzymes in milk has been reported (see Fox and McSweeney, 1996). Most of these originate from somatic cells, and their level increases during mastitic infection. The presence of cathepsin D, a lysozomal enzyme, in milk suggests that all the lysozomal proteinases are present in milk although they may not be active. These minor proteinases are considered to be much less significant than plasmin, but more work on the subject is necessary. [Pg.241]

Lysozome A membrane-bound organelle in the cytoplasm of most cells containing various hydrolytic enzymes that function in intracellular digestion... [Pg.111]

Cameron, T. I., Liten, A. D., Lawrence, J., Farenmark, J., and Turpen, T. H. (1998). Recovery of two recombinant human lysozomal enzymes from plant tissue by expanded bed adsorption with hydrophobic resins. Int. Conf. Expanded Bed Adsorption, 2nd, Napa Valley, CA, 1998, Abstr., p. 10.2. [Pg.430]

Substitution of Ca2+ by Ln3+ is achieved by soaking calcium containing crystals of the macromolecule in a solution of a lanthanide ion. Soaking times are two days in the case of thermolysin [79] and four weeks in the case lysozome [80]. [Pg.269]

The rotational frequency in lysozomes decreases with increase of water. This type of study throws some light on protein-micellar interactions and how they are affected by hydration. [Pg.195]

Weissman G, Bloomgarden D, Kaplan R, et al. A general method for introduction of enzymes by means of immmroglobulin-coated liposomes, into lysozomes of deficient cells. Proc Natl Acad Sci U S A 1975 72 88-92. [Pg.386]

Endoplasmic reticulum (ER) A membrane found within the cell that separates the cytoplasm from the lumen of the endoplasmic reticulum. Proteins destined to cross the plasma membrane, or to enter lysozomes, initially pass through the ER on their way to the Golgi apparatus. [Pg.918]

Cathepsin D. The indigenous acid proteinase in milk has received little attention. This activity was first recognized by Kaminogawa and Yamauchi (1972), who isolated and characterized the enzyme and considered it to be similar to the lysozomal acid proteinase, cathepsin D (EC 3.4.23.5). The presence of procathepsin D in milk has been reported (Larsen et al, 1993). Cathepsin D is relatively heat labile (completely inactivated by 70°C X 10... [Pg.214]

CS is an exciting and promising material in tissue regeneration applications as these biopolymers can be easily constructed into various forms and their derivatives are biodegradable by lysozomal enzymes. [Pg.117]


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See also in sourсe #XX -- [ Pg.380 , Pg.387 , Pg.393 ]




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Lysozomal enzymes

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