• Publications
  • Influence
Evolution in the structure and function of aspartic proteases
Aspartic proteases (EC3.4.23) are a group of proteolytic enzymes of the pepsin family that share the same catalytic apparatus and usually function in acid solutions. This latter aspect limits theExpand
  • 259
  • 8
Enzymic characteristics of secreted aspartic proteases of Candida albicans.
Candida yeasts are rarely infectious, but frequently cause life-threatening systemic infections in patients immunocompromised by AIDS or by immunosuppressive therapeutics. The secreted asparticExpand
  • 91
  • 7
Purification, characterization and partial amino acid sequencing of two new aspartic proteinases from fresh flowers of Cynara cardunculus L.
Two new aspartic proteinases have been isolated from stigmas of the cardoon Cynara cardunculus L. by a two-step purification procedure including extraction at low pH, gel filtration on Superdex 200,Expand
  • 139
  • 5
Cloning and Characterization of cDNA Encoding Cardosin A, an RGD-containing Plant Aspartic Proteinase*
Cardosin A is an abundant aspartic proteinase from pistils of Cynara cardunculus L. whose milk-clotting activity has been exploited for the manufacture of cheese. Here we report the cloning andExpand
  • 76
  • 5
  • PDF
Proteolytic activation of recombinant pro-memapsin 2 (pro-beta-secretase) studied with new fluorogenic substrates.
Memapsin 2 (beta-secretase), a membrane-anchored aspartic protease, is involved in the cleavage of beta-amyloid precursor protein to form beta-amyloid peptide. The primary structure of memapsin 2Expand
  • 60
  • 4
Purification and properties of cathepsin D from porcine spleen.
Cathepsin D was purified from porcine spleen to near homogeneity as determined by gel electrophoresis. The isolation scheme involved an acid precipitation of tissue extract, DEAE-cellulose andExpand
  • 63
  • 3
  • PDF
Complete amino acid sequence of streptokinase and its homology with serine proteases.
The complete amino acid sequence of streptokinase has been determined by automated Edman degradation of its cyanogen bromide and proteolytic fragments. The protein consists of 415 amino acidExpand
  • 141
  • 3
The crystal structure of bovine bile salt activated lipase: insights into the bile salt activation mechanism.
BACKGROUND The intestinally located pancreatic enzyme, bile salt activated lipase (BAL), possesses unique activities for digesting different kinds of lipids. It also differs from other lipases in aExpand
  • 80
  • 3
Conformational instability of the N‐ and C‐terminal lobes of porcine pepsin in neutral and alkaline solutions
Pepsin contains, in a single chain, two conformationally homologous lobes that are thought to have been evolutionarily derived by gene duplication and fusion. We have demonstrated that the individualExpand
  • 47
  • 3