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Lysine lysis

Homogenates of MetruUum senile, possibly the world s most common large sea anemone, yield extracts that are powerfully hemolytic for washed mammalian erythrocytes (22). The active substance, metridiolysin, is a protein of molecular weight approximately 80,000. In contrast to the sphingomyelin-inhibitable toxins, metridiolysin is an acidic protein having a pi of about 5. It is thermolabile and is inactivat by proteolytic enzymes. The optimal pH for hemolysis is between 5 and 6, and at pH 8 the lysin is inactive. It can be dissociated into two subunits of unequal size. Besides being cytolytic in vitro, metridiolysin is lethal when injected intravenously into mice. As shown in Table IV erythrocytes from the horse or dog are about a hundred times as sensitive to lysis as those from the mouse, and erythrocytes from other animals tested are intermediate in sensitivity. [Pg.308]

Thrombin activable fibrinolysis inhibitor (TAFI) is a plasma protein that is activated by thrombin in the presence of thrombomodulin to a labile carboxypeptidase-B-like enzyme that inhibits fibrinolysis. When TAFIa is included in a clot undergoing lysis induced by tPA and plasminogen, the time to achieve lysis is prolonged and free lysine and arginine are released (Wang et al., 1998). TAFIa retards the fibrin-enhanced activation of plasminogen by tPA and inhibits the accumulation of plasminogen at the lysis front (Sakharov et al., 1997). [Pg.276]

CjHjFjO 421-50-1) see Mefloquine A Mrifluoroacetyl-A -carboxy-L-Iysine anhydride (G)HmF4N204 42267-27-6) see Lisinopril A -(trifluoroacctyl)-L-lysine (C8H13F,N203 10009-20-8) see Lisinopril A" -(trifluornacetyI)-L-lysy]-L-proline (CnH FjNjOj 103300-89-6) see Lisinopril... [Pg.2449]

Lysine is an interesting exception The theoretical depletion point is not followed by further growth, but by prompt lysis and eventual disappearance of the culture. [Pg.143]

Fig. 1. A schematic representation of IgG depicting sites available for modification. Amino groups in the form of lysine residues may be scattered throughout the antibody. Arrows depict the sites of proteolytic lysis by papain and pepsin. Fig. 1. A schematic representation of IgG depicting sites available for modification. Amino groups in the form of lysine residues may be scattered throughout the antibody. Arrows depict the sites of proteolytic lysis by papain and pepsin.
Protein Concentration (mg/ml) Volume ( xl) for 50 xg Equalizing volume (lysis buffer) ( xl) Final volume for labeling CyDye (hi) Lysine (hO... [Pg.11]

Lysis is carried out in a disrupting device such as a French pressure cell. The preferred lysis buffer contains 100 mM Tris-HCl, pH 8.0 at 25°C, 0.5 M NaCl, 10 toM 2-mercaptoethanol, 50 xg/ml of phenylmethylsulfonyl fluoride (PMSF), 50 p,g/ml of iV-tosyl-L-phenylalanine chloromethyl ketone (TPCK), 50 (ig/ml of IV-a-tosyl-L-lysine chloromethyl ketone (TLCK), 50 (Jig/ml of pepstatin A, 50 p.g/ml of leupeptin, and 1 mM benzamidine. Typically, the cell sample is thawed in a water bath at room temperature in 1 ml of lysis buffer per 2 g of cells, and passed through a French pressure cell at 16,000 psi to produce a lysate. [Pg.182]

L-Lysine from acid-hydrolyzate (gr. lysis) of casein by E. Drechsel. Structure definitely established by synthesis by E. Fischer and F. Weigert 1902. [Pg.6]


See other pages where Lysine lysis is mentioned: [Pg.52]    [Pg.105]    [Pg.100]    [Pg.312]    [Pg.67]    [Pg.399]    [Pg.757]    [Pg.275]    [Pg.106]    [Pg.9]    [Pg.170]    [Pg.54]    [Pg.141]    [Pg.118]    [Pg.214]    [Pg.1272]    [Pg.39]    [Pg.45]    [Pg.757]    [Pg.190]    [Pg.30]    [Pg.104]    [Pg.366]    [Pg.39]    [Pg.6902]    [Pg.1245]    [Pg.81]    [Pg.565]    [Pg.84]    [Pg.1369]    [Pg.64]    [Pg.66]    [Pg.50]   
See also in sourсe #XX -- [ Pg.57 ]




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