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1 disease caused by a deficiency of the enzyme beta-mannosidase.
2  previously purified by Kengen et al., and a beta-mannosidase.
3                                              Beta-mannosidase, a lysosomal enzyme which acts exclusiv
4 nan requires endo-1,4-beta-mannanase and 1,4-beta-mannosidase activities.
5     Homozygous mutant mice have undetectable beta-mannosidase activity.
6 ilar gene organization with tomato endosperm beta -mannosidase and barley seed beta -glucosidase/ bet
7                             In addition, the beta-mannosidase and beta-glucosidase from P. furiosus b
8                                          The beta-mannosidase and beta-glucosidase genes were isolate
9 ity; however, this enzyme also exhibited 1,4-beta-mannosidase and cellodextrinase activities.
10    Based on these sequence similarities, the beta-mannosidase and the beta-glucosidase can both be cl
11 olecular masses of 59.0 and 54.6 kDa for the beta-mannosidase and the beta-glucosidase, respectively.
12 LysMan), core-specific alpha1,6-mannosidase, beta-mannosidase, and cleavage at the reducing terminus
13 nnosidase and barley seed beta -glucosidase/ beta -mannosidase BGQ60.
14         The complete sequence of the caprine beta-mannosidase cDNA coding region has been determined,
15                                            A beta-mannosidase could be known to hydrolyze beta-mannos
16 uenced the entire coding region of the human beta-mannosidase gene using a combination of cDNA librar
17 gues showed good and selective inhibition of beta-mannosidase (Helix pomatia).
18 etic analysis demonstrates that BtMan2A is a beta-mannosidase in which substrate binding energy is pr
19 e, alpha- and beta-galactosidase, alpha- and beta-mannosidase) in an assay that measured the rate of
20 otential treatment strategies, we produced a beta-mannosidase knockout mouse.
21 he beta-glucosidase, the primary role of the beta-mannosidase may not be disaccharide hydrolysis.
22                                          The beta-mannosidase showed optimal activity at pH 7.4 and 1
23 k the phosphate binding residues, are indeed beta-mannosidases that hydrolyze beta-1,2-mannosidic lin
24              The catalytic efficiency of the beta-mannosidase was significantly lower than that repor
25                   Km and Vmax values for the beta-mannosidase were determined to be 0.79 mM and 31.1

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