Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The tongue, pinna and dorsal skin of adult male C-1 mice were removed at 03.00, 06.00, 09.00, 12.00, 15.00, 18.00, 21.00 and 24.00 h, fixed in basic lead acetate and stained with Alcian blue-safranin or 0.5% toluidine blue. The mast cell numbers of these regions were counted and analyzed statistically by analysis of variance. It was found that there were circadian variations in the mast cell number in the tongue, pinna and dorsal skin. The difference between the minimum and maximum of circadian variation in mast cell number in all three regions was highly significant (p less than 0.01). Furthermore, the time points of the maximum and minimum of mast cell number varied between the different regions. The time point of the minimum in the tongue and pinna was at 06.00 h, whereas it was at 09.00 h in the dorsal skin. The time point of the maximum in the tongue and dorsal skin was at 21.00 h, but in the pinna it was at 18.00 h.
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PMID:Quantitative study of circadian variations in mast cell number in different regions of the mouse. 260 35

Effects of condensed tannins isolated from Rhei Rhizoma on the activities of angiotensin converting enzyme (ACE) and various proteases were examined in vitro. Among the various condensed tannins tested, procyanidin B-5 3,3'-di-O-gallate and procyanidin C-1 3,3',3"-tri-O-gallate strongly inhibited the activity of ACE. The concentration of procyanidin B-5 3,3'-di-O-gallate required for 50% inhibition of ACE was 1.3 X 10(-6) M. The inhibition of ACE by condensed tannins was reversible and non-competitive, according to dialysis and to Dixon plots. However, over one hundred times the concentration was required to inhibit activities of other proteases such as trypsin, chymotrypsin, leucine aminopeptidase, carboxypeptidase A and urinary kallikrein. These results suggest that the inhibitory effects of condensed tannins on the activities of ACE are specific.
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PMID:Inhibitory effects of condensed tannins on angiotensin converting enzyme. 303 68

Catechol 1,2-dioxygenase (pyrocatechase) has been purified to homogeneity from Pseudomonas putida mt-2. Most properties of this enzyme, such as the absorption spectrum, iron content, pH stability, pH optimum, substrate specificity, Km values, and amino acid composition, were similar to those of catechol 1,2-dioxygenase obtained from Pseudomonas arvilla C-1 [Y. Kojima et al. (1967) J. Biol. Chem. 242, 3270-3278]. These two catechol 1,2-dioxygenases were also found, from the results of Ouchterlony double diffusion, to share several antigenic determinants. The molecular weight of the putida enzyme was estimated to be 66,000 and 64,000 by sedimentation equilibrium analysis and Sephadex G-200 gel filtration, respectively. The enzyme gave a single band on sodium dodecyl sulfate-polyacrylamide gel electrophoresis, corresponding to Mr 32,000. The NH2-terminal sequence, which started with threonine, was determined up to 30 residues by Edman degradation. During the degradation, a single amino acid was released at each step. The NH2-terminal sequence up to 20 residues was identical to that of the beta subunit of the arvilla enzyme, with one exception at step 16, at which arginine was observed instead of glutamine. The COOH-terminal residue was deduced to be arginine on carboxypeptidase A and B digestions and on hydrazinolysis. These results indicate that the putida enzyme consists of two identical subunits, in contrast to the arvilla enzyme which consists of two nonidentical subunits, alpha and beta [C. Nakai et al. (1979) Arch. Biochem. Biophys. 195, 12-22], although these two enzymes have very similar properties.
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PMID:Purification and properties of catechol 1,2-dioxygenase (pyrocatechase) from Pseudomonas putida mt-2 in comparison with that from Pseudomonas arvilla C-1. 321 77

Treatment of the purple membrane with carboxypeptidase A, Pronase, or papain, results in the cleavage of amino acids from the carboxyl terminus of bacteriorhodopsin, a maximum of about 17 amino acids being released with papain. Protease-treated bacteriorhodopsin, after denaturation, refolds to the native structure, binds retinal as tightly as the intact protein and, on reconstitution into vesicles, gives full proton translocating activity. The CD spectrum of papain-treated purple membrane shows exciton coupling characteristic of the intact purple membrane. The trimeric bacteriorhodopsin in papain-treated purple membrane dissociates into monomers in Triton X-100 which, after removal of the detergent, reassociate to form the oligomeric structures. Chymotrypsin cleaves papain-treated bacteriorhodopsin between amino acids 71 and 72 as has been previously found for intact bacteriorhodopsin. The resulting fragments C-1 (amino acids 72-231) and C-2 (amino acids 1-71) reassociate, bind retinal, and regenerate the native chromophore, as previously demonstrated for the corresponding fragments from the intact protein. We conclude that the COOH-terminal peptide in bacteriorhodopsin is not required for the correct refolding of denatured bacteriorhodopsin to the native tertiary and quarternary structure, for chromophore regeneration or for light-driven proton translocation.
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PMID:Removal of the carboxyl-terminal peptide does not affect refolding or function of bacteriorhodopsin as a light-dependent proton pump. 670

Gamma-thujaplicin, beta-dolabrin and hinokitiol(beta-thujaplicin), hinokitiol-related compounds isolated from the wood of Thujopsis dolabrata S. and Z. hondai MAK have antimicrobial activity. In particular, strong antibacterial activity of hinokitiol and beta-dolabrin on Staphylococcus epidermidis IFO-12993 was found, with a minimum inhibitory concentration (MIC) of 0.2 microg/ml. This activity was higher than that of gentamicin, used as a positive control, and so the strong antibacterial activity of both compounds on this bacterium is of considerable interest. Of the three compounds, gamma-thujaplicin showed the strongest antifungal activity and its MIC was found to be around 1.5 microg/ml. The three compounds also inhibited metalloproteases. The inhibitory activity of hinokitiol on carboxypeptidase A was especially strong, its 50%-inhibitory concentration (IC50) being 2.76x10(-6) M. Considering that metalloproteases are involved in inflammation, the strong inhibitory activity of hinokitiol could be important. On the other hand, hinokitiol-acetate did not show any antimicrobial activity and metalloprotease inhibition, suggesting that at least part of the activity is due to metal chelation between the carbonyl group at C-1 and the hydroxyl group at C-2 in the tropolone skeleton.
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PMID:Antimicrobial activity and metalloprotease inhibition of hinokitiol-related compounds, the constituents of Thujopsis dolabrata S. and Z. hondai MAK. 1051 29