| pubmed-article:10705615 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10705615 | lifeskim:mentions | umls-concept:C0579233 | lld:lifeskim |
| pubmed-article:10705615 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:10705615 | lifeskim:mentions | umls-concept:C0020196 | lld:lifeskim |
| pubmed-article:10705615 | lifeskim:mentions | umls-concept:C1534709 | lld:lifeskim |
| pubmed-article:10705615 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10705615 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:10705615 | pubmed:dateCreated | 2000-4-13 | lld:pubmed |
| pubmed-article:10705615 | pubmed:abstractText | A hyaluronic acid splitting enzyme of Streptococcus agalactiae was characterized by splitting mechanism, Michaelis-constant and inhibition type for sulfated hyaluronic acid: The enzyme splits hyaluronic acid as a hyaluronate lyase [EC 4.2.2.1]. The Km = 8 x 10(-4) mg ml-1 was determined with the influence of substrate inhibition constant Kiu = 2 x 10(-6) mg ml-1. Sulfated hyaluronic acid inhibits the enzyme in a partially non-competitive way. The inhibition constant is Ki = 5.47 x 10(-4) mg ml-1. The GBS-hyaluronate lyase cleaves hyaluronic acid as an endoglycosidase. The work is related with the intention to establish a hyaluronate lyase of microbial origin as a therapeutical enzyme replacing bovine hyaluronidase. | lld:pubmed |
| pubmed-article:10705615 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10705615 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10705615 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10705615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10705615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10705615 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10705615 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10705615 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10705615 | pubmed:issn | 0934-8840 | lld:pubmed |
| pubmed-article:10705615 | pubmed:author | pubmed-author:MüllerP JPJ | lld:pubmed |
| pubmed-article:10705615 | pubmed:author | pubmed-author:PeschelGG | lld:pubmed |
| pubmed-article:10705615 | pubmed:author | pubmed-author:RodinAA | lld:pubmed |
| pubmed-article:10705615 | pubmed:author | pubmed-author:OzegowskiJ... | lld:pubmed |
| pubmed-article:10705615 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10705615 | pubmed:volume | 289 | lld:pubmed |
| pubmed-article:10705615 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10705615 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10705615 | pubmed:pagination | 835-43 | lld:pubmed |
| pubmed-article:10705615 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:meshHeading | pubmed-meshheading:10705615... | lld:pubmed |
| pubmed-article:10705615 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10705615 | pubmed:articleTitle | Complementary characterization of a hyaluronic acid splitting enzyme from Streptococcus agalactiae. | lld:pubmed |
| pubmed-article:10705615 | pubmed:affiliation | Hans-Knöll-Institut für Naturstoff-Forschung e.V., Jena, Germany. | lld:pubmed |
| pubmed-article:10705615 | pubmed:publicationType | Journal Article | lld:pubmed |
