These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Further characterization of buffalo spleen cathepsin B.
    Author: Ahmad S, Khan MY.
    Journal: Biochem Int; 1990 Dec; 22(6):951-8. PubMed ID: 2090108.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]