| pubmed-article:20158206 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:20158206 | lifeskim:mentions | umls-concept:C0005304 | lld:lifeskim |
| pubmed-article:20158206 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:20158206 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:20158206 | lifeskim:mentions | umls-concept:C0917787 | lld:lifeskim |
| pubmed-article:20158206 | lifeskim:mentions | umls-concept:C0998219 | lld:lifeskim |
| pubmed-article:20158206 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:20158206 | pubmed:dateCreated | 2010-3-17 | lld:pubmed |
| pubmed-article:20158206 | pubmed:abstractText | The effects of betaine on prawn beta-N-acetyl-D-glucosaminidase (NAGase) activity for the hydrolysis of p-nitrophenyl-N-acetyl- beta-D-glucosaminide (pNP-NAG) have been studied. The results showed that appropriate concentrations of betaine could lead to reversible inhibition against NAGase, and the IC(50) value was estimated to be 15.00 +/- 0.30 mM. The inhibitory kinetics assay showed that betaine was a mixed type inhibitor with a K(I) value of 9.17 +/- 0.85 mM and a K(IS) value of 45.58 +/- 2.52 mM. The inhibitory model was set, and the microscopic rate constants were determined using the kinetic method of the substrate reaction. The time course of the hydrolysis of pNP-NAG catalyzed by NAGase in the presence of different betaine concentrations showed that at each betaine concentration, the rate decreased with an increase in time until a straight line was approached, indicating that the inhibition of NAGase by betaine is a slow, reversible reaction with fractional residual activity. The fact that k(+0) is much larger than k(+0)(') indicated that the free enzyme molecule is more fragile than the enzyme-substrate complex against betaine. It is suggested that the presence of the substrate offers marked protection of NAGase against inhibition by betaine. | lld:pubmed |
| pubmed-article:20158206 | pubmed:language | eng | lld:pubmed |
| pubmed-article:20158206 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20158206 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:20158206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20158206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20158206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:20158206 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:20158206 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:20158206 | pubmed:issn | 1520-5118 | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:ZhouHan-TaoHT | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:WangYeY | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:ChenQing-XiQX | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:XieXiao-LanXL | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:YanJiang-HuaJ... | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:WeiXiao-QianX... | lld:pubmed |
| pubmed-article:20158206 | pubmed:author | pubmed-author:HuangQian-She... | lld:pubmed |
| pubmed-article:20158206 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:20158206 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:20158206 | pubmed:volume | 58 | lld:pubmed |
| pubmed-article:20158206 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:20158206 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:20158206 | pubmed:pagination | 3820-4 | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:meshHeading | pubmed-meshheading:20158206... | lld:pubmed |
| pubmed-article:20158206 | pubmed:year | 2010 | lld:pubmed |
| pubmed-article:20158206 | pubmed:articleTitle | Inhibitory kinetics of betaine on beta-N-acetyl-D-glucosaminidase from prawn (Litopenaeus vannamei). | lld:pubmed |
| pubmed-article:20158206 | pubmed:affiliation | Key Laboratory of the Ministry of Education for Coastal and Wetland Ecosystems, School of Life Sciences, Xiamen University, Xiamen, China. | lld:pubmed |
| pubmed-article:20158206 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:20158206 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
