Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
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Drug
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Target Concepts:
Gene/Protein
Disease
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Drug
Enzyme
Compound
Query: EC:3.4.21.4 (
trypsin
)
42,187
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
Murine resident macrophages express, on their surface, carbohydrate epitopes which undergo changes during their stimulation/activation as monitored by binding of 125I labelled Evonymus europaea and Griffonia simplicifolia I-B4 lectins. Treatment of the stimulated macrophages with coffee bean
alpha-galactosidase
abolished binding of the GS I-B4 isolectin and changed the binding pattern of the Evonymus lectin. The affinity (Ka) of Evonymus lectin for
alpha-galactosidase
-treated macrophages decreased approximately 23-fold, from 1.25 x 10(8) M-1 to 5.5 x 10(6) M-1. Subsequent digestion of
alpha-galactosidase
-treated macrophages with alpha-L-fucosidase from Trichomonas foetus, further reduced binding of Evonymus lectin. Resident macrophages showed the same pattern of Evonymus lectin binding, with the same affinity, as
alpha-galactosidase
-treated, stimulated macrophages. These results, together with a consideration of the carbohydrate binding specificity of the Evonymus lectin which, in the absence of alpha-D-galactosyl groups, requires alpha-L-fucosyl groups for binding, indicate the presence, on resident macrophages, of glycoconjugates with terminal alpha-L-fucosyl residues. It is also concluded that during macrophage stimulation/activation alpha-D-galactosyl residues are added to this glycoconjugate and that they form part of the receptor for Evonymus lectin. The same glycoconjugate(s) is/are also expressed on the activated macrophage IC-21 cell line which exhibits the same characteristics as that of stimulated peritoneal macrophages, i.e., it contains alpha-D-galactosyl end groups and is resistant to the action of
trypsin
. Both lectins were also specifically bound to Corynaebacterium parvum activated macrophages.
...
PMID:Alpha-D-galactosylation of surface fucoglycoconjugate(s) upon stimulation/activation of murine peritoneal macrophages. 134 14
Endocytotic internalization of
alpha-galactosidase
by cultured fibroblasts derived from a patient with Fabry's disease was achieved via receptor-mediated endocytosis of alpha-2-macroglobulin (alpha-2-M).
alpha-galactosidase
of coffee beans was conjugated to alpha-2-M when the latter was treated with
trypsin
. Internalization of the conjugate resulted in an increase of
alpha-galactosidase
activity in the crude cell extracts. The observed internalization was blocked by the presence of bacitracin, an inhibitor of binding between alpha-2-M and its receptor on the cell surface. When the cells were incubated at 4 degrees C with the conjugate, internalization was also inhibited. The
alpha-galactosidase
activity in the cells was saturated when the concentration of the conjugate in the medium was 40 micrograms/ml. Since non-conjugated
alpha-galactosidase
was not effectively internalized, the observed internalization of the conjugate was mediated by recognition of alpha-2-M by its receptor. The effective internalization of
alpha-galactosidase
described in this paper has a potential use in the enzyme replacement therapy of Fabry's disease.
...
PMID:Endocytotic internalization of alpha-2-macroglobulin: alpha-galactosidase conjugate by cultured fibroblasts derived from Fabry hemizygote. 243 88
The enzymatic activities of 53 strains of Pseudomonas cepacia were determined by using the API ZYM system. Strong alkaline phosphatase, acid phosphatase, butyrate esterase, caprylate esterase, myristate lipase, leucine arylamidase, and phosphoamidase activities were consistently detected in all strains. Weak activities were observed for valine arylamidase, beta-glucosidase, and N-acetyl-beta-glucosaminidase. No activities could be demonstrated for cystine arylamidase,
trypsin
, chymotrypsin,
alpha-galactosidase
, beta-galactosidase, beta-glucuronidase, alpha-glucosidase, alpha-mannosidase, and alpha-fucosidase. Enzymatic activities of pseudomonads may provide useful information about their pathogenesis and information for identification of Pseudomonas species.
...
PMID:Enzymatic characterization of Pseudomonas cepacia by API ZYM profile. 335 98
For comparative studies we have used the somatic cell hybridization approach to regionally map genes on the mouse X chromosome. Fibroblasts from a mouse with the balanced reciprocal translocation T(XD;16B5)16H were fused with a Chinese hamster cell line (V79/380-6) deficient in activity of the enzyme hypoxanthine phosphoribosyltransferase (HPRT). Interpecific cell hybrids were initially selected for retention of the mouse translocation chromosome carrying the Hprt gene. Subsequently, hybrid clones were counterselected to force segregation of this chromosome. Selected and counterselected hybrid clones were analyzed for their chromosome content by
trypsin
/Giemsa banding and for expression of the mouse forms of the X-linked enzymes HPRT and
alpha-galactosidase
(GALA) by isoelectric focusing. The results indicate that the breakpoint on the mouse X chromosome (in band XD) has separated the genes for HPRT (Hprt) and for GALA (Ags). Hprt is proximal to the breakpoint in region Xcen-XD and Ags is distal in region XD-Xter. The gene order in the mouse (centromere-Hprt-Ags) is therefore inverted when compared to the order of the homologous loci on the long arm of the human X (centromere-GALA-HPRT).
...
PMID:Comparative gene mapping: order of loci on the X chromosome is different in mice and humans. 625 72
The enzymatic profiles of several yeastlike organisms were studied using 19 substrates included in the API ZYM system. The isolates evaluated were: 186 Candida albicans, 19 C. stellatoidea, 4 C. tropicalis, 2 C. parapsilosis, 2 C. pseudotropicalis, 1 C. guilliermondii, 3 C. krusei, 11 Torulopsis (Candida) glabrata, 1 Cryptococcus neoformans, 2 Saccharomyces carlsbergensis, 1 Rhodotorula rubra, and 1 R. mucilaginosa. Esterase lipase (C8), leucine arylamidase, acid phosphatase, and phosphoamidase were detected in all of the isolates while
trypsin
and
alpha-galactosidase
were not found in any of the isolates using this system. The other enzymes were produced to a variable degree. The different enzymatic profiles might prove useful in the rapid differential diagnosis of genera and species of these yeastlike organisms. To this end, more extensive studies using more isolates of each species will be required, and enzymatic activity should be verified with other techniques and substrates.
...
PMID:Contribution to the study of the enzymatic profiles of yeast organisms with medical interest. 631 Apr
This paper presents data on reactions of murine macrophages with a variety of lectins, with special focus on Griffonia simplicifolia I-B4 isolectin, the only lectin we tried that distinguishes stimulated macrophages from resident populations. Specificity of Griffonia simplicifolia I reaction with carbohydrate determinants at the cell surface is shown by (i) ability of
alpha-galactosidase
treatment of intact cells to abolish all lectin binding whereas beta-galactosidase has no effect on lectin binding, (ii) ability of methyl alpha-D-galactopyranoside to completely inhibit lectin binding with methyl alpha-D-galactopyranoside having no effect on lectin binding, (iii) ability of brief treatment of intact cells with
trypsin
to liberate a glycopeptide but reacts with G. simplicifolia I to form a precipitate that is dissolved by addition of methyl-alpha-D-galactopyranoside or
alpha-galactosidase
, (iv) ability of methyl alpha-D-galactopyranoside (but no other monosaccharide) to completely inhibit avid binding of macrophages to G. simplicifolia I lectin immobilized on an insoluble support, and (v) ability of immobilized lectin to separate macrophages into highly pure subpopulations of lectin-reactive and lectin-unreactive cells, as shown by examination of fluorescein-labeled lectin-treated cells with phase-contrast/fluorescence microscopy.
...
PMID:Stimulated macrophages express a new glycoprotein receptor reactive with Griffonia simplicifolia I-B4 isolectin. 679 67
Enzymatic characterization of 48 Aeromonas hydrophila complex isolates from various sources was determined with the API ZYM system (Analytab Products, Plainview, N.Y.). All isolates lacked valine and cystine aminopeptidases, chymotrypsin, alpha-mannosidase, alpha-fucosidase,
alpha-galactosidase
, and beta-glucuronidase but possessed caprylate esterase-lipase, leucine aminopeptidase, acid phosphatase, phosphoamidase, and N-acetyl-beta-glucosidase. Variability was found in the presence of alkaline phosphatase, butyrate esterase, myristate lipase,
trypsin
, beta-galactosidase, alpha-glucosidase, and beta-glucosidase. No significant differences were evident among the enzymatic profiles of isolates from various sources.
...
PMID:Enzymatic characterization of Aeromonas hydrophila complex by the API ZYM system. 681 46
Ninety-nine strains of Gram-negative black-pigmented anaerobic rods, grown on Todd-Hewitt blood agar plates, were identified and characterized according to a typing scheme including UV fluorescence, catalase,
trypsin
-like and haemagglutinating activities, biochemical tests with the ATB 32A kit, and gas-liquid chromatography. To determine the taxonomic position of the Porphyromonas gingivalis biotypes, 68 strains (31 of human origin and 37 of animal origin) were compared to 31 strains of closely related species or of uncertain generic status. Most animal strains were isolated in our laboratory by subculturing samples from the oral cavity of five mammalian species (bear, cat, coyote, dog and wolf). Those strains differed from human P. gingivalis strains in that they were positive for catalase, beta-galactosidase and glutamyl-glutamic acid arylamidase; from Bacteroides macacae by more rapid pigmentation, positive haemagglutination, failure to produce propionic acid, and negative
alpha-galactosidase
; and from Bacteroides salivosus by more rapid pigmentation, positive haemagglutination and failure to produce propionic acid. These data demonstrate that phenotypic heterogeneity within the taxon P. gingivalis can be resolved into two biotypes, each corresponding to a human source or an animal source.
...
PMID:Phenotypic characterization of human and animal biotypes within the species Porphyromonas gingivalis. 819 Sep 90
An epidemiologic study of Pasteurella haemolytica serovar 1 (Ph1) in market-stressed feeder calves from 7 farms in eastern Tennessee was conducted. The nasal mucus of each calf was cultured sequentially at the farm of origin (day 0), at an auction market (day 133), and at a feedyard in Texas (days 141, 148, 155, and 169). Of the 103 calves tested, 77 were culture-positive, including 1 on day 0, 1 on day 133, 20 on day 141, 57 on day 148, 50 on day 155, and 14 on day 169. From the 143 Ph1 isolates, 20 enzyme profiles were determined by use of a commercial enzyme system that detects 19 enzymatic reactions; 4 antimicrobial susceptibility profiles were obtained, using the disk-diffusion method, which evaluated susceptibility to 11 antibacterial drugs. All isolates were positive for acid phosphatase and alkaline phosphatase, but were negative for
alpha-galactosidase
, alpha-mannosidase, beta-glucosidase, beta-glucuronidase, cystine aminopeptidase, N-acetyl-beta-glucosaminidase, and
trypsin
. Other positive enzyme reactions included: leucine aminopeptidase, 140 Ph1 isolates; phosphohydrolase, 90 isolates; alpha-fucosidase, 63 isolates; esterase (C4), 59 isolates; valine aminopeptidase, 30 isolates; esterase lipase (C8), 24 isolates; beta-galactosidase, 2 isolates; and alpha-glucosidase, chymotrypsin and lipase (C14), 1 isolate each. Thirty-four Ph1 profiles were identified, using combined enzyme and antimicrobial susceptibility profiles. The data indicate that the strains isolated during the feedyard period may have been determined more by farm of origin (P < or = 0.001) than by habitation with calves from other farms while in the feedyard.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Identification of Pasteurella haemolytica A1 isolates from market-stressed feeder calves by use of enzyme and antimicrobial susceptibility profiles. 842 78
The enzymatic activity of 70 feline and canine Microsporum canis isolates was determined by the Api-Zym test. The liquid phase of cultures, inoculated into Tryptic Soy Broth, was used to examine 19 enzymes. Considerable differences were observed among the extracellular enzymatic patterns. All the isolates produced alkaline phosphatase and beta-glucosidase, while lipase (C14),
trypsin
, chymotrypsin, beta-glucuronidase, and alpha-fucosidase activity was never revealed. Esterase (C4) activity was present in 57 samples (81%), esterase lipase (C8) in 31 (44%), leucine arylamidase in 35 (50%), valine arylamidase and cystine arylamidase in 7 (10%), acid phosphatase in 64 (91%), naphthol-AS-BI-phosphohydrolase in 60 (86%),
alpha-galactosidase
in 5 (7%), beta-galactosidase in 6 (8%), alpha-glucosidase in 25 (36%), N-acetyl-beta-glucosaminidase in 41 (58%), and alpha-mannosidase in 51 (73%). The beta-galactosidase activity of M. canis has not been reported previously. Remarkable variations of intensity for each enzymatic activity were also detected. It is believed that these results could provide basic data for further investigations on the pathogenic role of enzymes secreted by M. canis.
...
PMID:Extracellular enzymatic activity of Microsporum canis isolates. 868 26
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