Linked Life Data

2090108

Source:http://linkedlifedata.com/resource/pubmed/id/2090108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1991-5-28
pubmed:abstractText
Cathepsin B (EC 3.4.22.1) from buffalo spleen was isolated to homogeneity and its molecular weight was determined to be 25 KDa. The enzyme was found to be a glycoprotein having a total carbohydrate content of 7%. The NH2- and COOH-terminal amino acid residues were identified as Leu and Thr, respectively. The specific extinction coefficient, E1%1cm, of the enzyme was determined to be 13.2. The value of intrinsic viscosity and equivalent hydrodynamic radius of the enzyme were calculated to be 3.47 ml/gm and 2.34 nm, respectively. Polyclonal antibodies raised in rabbits were found to cross-react distinctly with the purified buffalo enzyme. Using BANA as substrate, the Km and Vmax values were determined to be 0.93 mM and 5.57 Units/mg, respectively. The buffalo enzyme was also found to be highly active against protein substrates, and the Km values for casein and BSA were measured to be 1.12 and 1.74 microM, respectively.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0158-5231
pubmed:author
pubmed:issnType
Print
pubmed:volume
22
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
951-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Further characterization of buffalo spleen cathepsin B.
pubmed:affiliation
Department of Biochemistry, School of Life Sciences, North-Eastern Hill University, Shillong, India.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't