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Protein tests

Rifai N, Warnick GR, Dominiczak MH, eds. (1997) Handbook of protein testing. AACC Press, Washington. [Pg.234]

Homologous proteins Testing purified animal Data should be interpreted... [Pg.437]

Another potential class of antivirals is those that interfere with the ability of virus to enter cells. If the virus entry process is inhibited, then spread of infection within an individual might be inhibited. As discussed earlier, HIV virus particles initially attach to cells by way of the cellular receptor for CD4 protein, which is embedded in the surface of normal T lymphocytes and macrophages. Recently, recombinant DNA techniques have been used to make large amounts of a part of the pure CD4 protein. Test-tube experiments have shown that if this CD4 protein fragment is incubated with T lymphocytes or macrophages, it can saturate all the CD4 receptors and prevent subsequent infection with HIV. It is possible that this approach might be effective in people, as well. [Pg.236]

The coiled-coil domain frequently mediates hetero- or homodimerization. About two-thirds of a large number of TRIM proteins tested dimerize [125]. As a number of other RING finger proteins either homo- or hererodimerize, dimerization may facilitate optimal E3 activity of TRIMs. While most proteins that carry the TRIM... [Pg.60]

The effect of dietary protein on diazinon toxicity was evaluated in a study with male albino Wistar rats. The study concluded that a purified protein test diet (with 26% casein and 59% cornstarch) did not significantly alter the LD50 value (415 mg/kg) for diazinon for this species. However, a low protein purified test diet (3.5% casein, 82% cornstarch), lowered the LD50 to 215 mg/kg. In addition, this study found that diazinon samples that were time-of-manufacture stabilized (to prevent spontaneous degradation to more toxic monothiotetraethyl pyrophosphate) were less toxic (LD50 value = 466 mg/kg) than samples stabilized after manufacture (LD50 value = 271 mg/kg) (Boyd and Carsky 1969). A subsequent study... [Pg.32]

The separation of protein test mixtures on very short C 8 columns yielded surprising results (Fig. 18). The resolution obtained with a 6.3 x 4.6 mm column was about 2.25 or 2.22 times better than with a 45 x 4.6 mm column when the flow rate was low (0.25 or 0.5 ml/min, respectively) and the volumetric gradient rate large (16% B/ml). The gradient components were A water and B 2-propanol, both with 0.1% trifluoro-acetic acid (TFA)73). Even a column (better to say, a disk) 1.6 mm in length and 4.1 mm in diameter was effective in separating ribonuclease A, cytochrome C, and ovalbumin. Of course, the sample capacity of such a short column was very low 73). [Pg.189]

Protein tested Ratios obtained with the BCA method Ratios obtained with the Coomassie plus method Ratios obtained with the modified Lowry method... [Pg.99]

For metabolic fecal nitrogen determination, fecal nitrogen from a zero-protein test group must also be determined. [Pg.127]

Calibrate pH meter at 37°C. Equilibrate casein solution (control) to pH 8 0.03 by adding either dilute NaOH or HC1. Repeat for protein test solutions (see Basic Protocol 3). Hold both control and test protein solutions at 37°C. [Pg.132]

PER test group diet formula. Diet for test group with the protein fraction for thediet being the protein of interest (i.e., test protein) Test diets are 10% protein. The protein ingredient... [Pg.135]

Protein determination by the Kjeldahl method is slow and very few samples can be run at one time. The Lowry and many other protein tests are much more convenient. A Lowry assay on a test tube rack of 40 samples can be done in <2 hr. [Pg.323]

Four bioassays a) 30 min acute bacterial test (Vibrio fischeri) b) 72h algal test (Pseudokirchneriella subcapitata) c) 7d chronic crustacean test (Ceriodaphnia dubia) d) 48h acute crustacean test (Daphnia magna) and in vitro induction stress protein test (HELA- hsp-CAT cells) Different industrial waste leachates Decantation, 100 pm filtration followed by 5.5-8.5 pH adjustment (for daphnid test), followed by 0.45 pm filtration (for other tests)... [Pg.345]

This marked enzymic activity was exhibited by the preparation at a dilution of 1 100,000,000 parts of water. The most delicate tests for proteins are not valid at dilutions greater than about 1 100,000. Our preparation reacted like typical protein to the usual protein tests, but its own enzymic activity constituted a test for its presence which was 1000 times more delicate. Thus the f ailure of protein reactions in solutions enzymically active does not show that the enzyme is of other than protein nature in its chemical composition, although this negative conclusion has been erroneously drawn by some investigators and is repeated by many writers. [Pg.2]

The endogenous HMG-domain proteins in HeLa cell free extracts do not seem to affect the relative rates of repair of cisplatin-DNA adducts [54] [62], Nevertheless, the hypothesis that HMG-domain proteins can enhance cellular sensitivity to cisplatin by blocking repair of the DNA adducts is still viable. Several HMG-domain proteins are specifically expressed in the testes ([146] and references cited therein), two of which, tsHMG and hSRY, inhibit the in vitro excision of cisplatin-DNA adducts at lower protein concentrations than any of the other HMG-domain proteins tested [54] [146], Selective expression of these or other such proteins in testicular tumors would provide an explanation for the unusual cisplatin sensitivity of this tumor type and the reduced repair of cisplatin-DNA adducts observed in testicular cell lines (discussed above). [Pg.93]

The smallest vertebrates are homogenized whole and most laiger animals can be dissected and different tissues removed for storage in 1.5-ml Eppendorf microtubes at — 70° until homogenized. Heart, kidneys, or liver are sufficient to score more than 20 proteins testes, spleen, brain, and muscle can be sampled for tissue-specific enzymes. Additionally, blood, muscle, and/or saliva from most vertebrates can be conveniently sampled without killing the animal. During all sample preparation steps, keep tubes on crushed ice. [Pg.99]

Purpose To evaluate the toxicology of a protein test article in a nonrodent species after every-other-day subcutaneous dosing for 28 days. [Pg.442]

Capillary SDS-gel electrophoresis is a rapid automated separation and characterization technique for protein molecules and is contemplated as a modern instrumental approach to sodium dodecylsulfate-polyacrylamide slab-gel electrophoresis (SDS-PAGE). Size separation of SDS-protein complexes can be readily attained in coated capillaries filled with cross-linked gels or non-cross-linked polymer networks. Figure 9 depicts one of the early applications of the technique for the analysis of a standard protein test mixture ranging in size from 14.2 to 205 kDa. [Pg.91]


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