Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P04040 (Catalase)
 3,577 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Thirty-nine strains of gram-positive microaerophilic cocci isolated from cases of heifer and dry-cow mastitis were biochemically characterized with the API 50E and API-ZYM test kit systems, gas-liquid chromatography for analysis of end products of glucose metabolism, and anaerobic biochemical tests (L. V. Holdeman, E. P. Cato, and W. E. C. Moore, Anaerobe Laboratory Manual, Virginia Polytechnic Institute, Blacksburg, 1977). Strains were screened for production of a variety of extracellular enzymes on substrate-containing agar plates and for hemolysin and coagulase production. Antibiotic susceptibility and sensitivity tests were also performed. The microaerophilic cocci displayed homogeneity with respect to the majority of the biochemical tests used; i.e., greater than or equal to 90% of the strains were consistently positive or negative in any one test and probably represent one species. All produced deoxyribonuclease, ribonuclease, and hyaluronidase, and 92% were positive for chondroitin sulfatase. Catalase and coagulase tests were negative. Greening was observed on bovine blood agar. Acetic and succinic acids were produced by all strains as the only detectable products of glucose metabolism. The strains were susceptible to penicillin G, cefoxitin, doxycycline, and chloramphenicol and were resistant to clindamycin, novobiocin, and metronidazole. Their taxonomic position remains unclear.
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PMID:Biochemical characterization of unidentified microaerophilic cocci isolated from heifer and dry-cow mastitis. 39 19

One theory suggests that by maintaining the protein in an amorphous glassy sugar matrix, the physical hindrance encountered by the protein functions to stabilize it. Thus, the nature of the sugar/protein interaction is important as is the maintenance of the sugar in an amorphous form without any recrystallization. Moisture is known to function as a plasticizer and facilitate crystallization and thus loss of the amorphous state. We report the effect of cospray-drying with different proteins on the physical stability of lactose and mannitol. Particle sizing showed their suitability for inhalation, and the effect of exposure of the spray-dried products to moisture vapor was monitored gravimetrically. Bovine liver catalase, bovine pancreatic insulin, and bovine pancreatic ribonuclease A when individually cospray-dried with lactose showed no extensive initial crystallinity by powder X-ray diffraction, but proteins cospray-dried with mannitol generally showed evidence of mannitol component crystallinity. Catalase appeared to inhibit lactose crystallization from an amorphous matrix to a greater extent than insulin when exposed to short-term elevated humidity, but this difference was a kinetic feature. The hygroscopicities of the cospray-dried materials differed and indicated that each protein/sugar system required individual characterization to identify an optimal formulation.
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PMID:Water vapor sorption studies on the physical stability of a series of spray-dried protein/sugar powders for inhalation. 981 83

Agricultural production is becoming increasingly dependent on the environmental factors that alter soil properties, plant productivity, and product quality. Environment pollution caused by heavy metals because of human activities are among the most dangerous pollutants on the biosphere. Here, we have studied the biochemical adaptation of wild and cultivated soybeans to the simulated effects of lead nitrate and lead acetate. Lead in the form of acetate had a relevant toxic effect, as evidenced by a significant increase in the concentration of malonic dialdehyde in the treated samples relative to control samples. Catalase and peroxidase, possibly performing a signaling function, are involved in the adaptation to the toxicity of Pb salts. The studied Pb salts showed a predominant stimulating effect on the specific activity of acid phosphatases in cultivated soybean, while the ribonuclease activity changed in both Glycine species. Moreover, in wild soybean, it was mostly suppressive, except for the first day. We found that the electrophoretic spectra of acid phosphatases of soybean seedlings was highly stabile, while that of ribonucleases varied depending on the salt. On the seventh day of exposure, lead nitrate caused a decrease in the specific activity of the studied hydrolases of seedlings of cultivated and wild soybeans. A change in the number or electrophoretic mobility of multiple forms of enzymes during treatment with Pb salts was revealed, which indicates the adaptation of the plants at the molecular genetic level. These results imply that the observed enzymes can be used as sensitive indicators for predicting the effects of heavy metals on soybean.
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PMID:Biochemical adaptation of wild and cultivated soybean against toxicity of lead salts. 3247 23