Results 121 to 130 of about 13,055 (147)

Comparison of Two Cysteine Endopeptidases from Pseudananas macrodontes (Morr.) Harms (Bromeliaceae)

Biological Chemistry, 2001
The properties of two cysteine peptidases (macrodontain I and II) isolated from fruits of Pseudananas macrodontes have been compared. The enzymes showed optimum pH ranges near neutrality and were inhibited by E-64 and other cysteine peptidase inhibitors.
Laura M I Lopez, Sebastian A Trejo, Nestor O Caffini   +2 more
exaly   +3 more sources

[38] Pineapple cysteine endopeptidases

Methods in Enzymology, 1994
Andrew D Rowan, David J Buttle, A D Rowan   +2 more
exaly   +2 more sources

Trematode Cysteine Endopeptidases

2013
Mark W Robinson, Paul J Brindley, John P Dalton   +2 more
exaly   +2 more sources

[35] Cysteine endopeptidases of Entamoeba histolytica

Methods in Enzymology, 1994
Henning Scholze, Egbert Tannich
exaly   +2 more sources

Cysteine Endopeptidases

2008
exaly   +2 more sources

Histolysain and Other Entamoeba Cysteine Endopeptidases

2013
H Scholze, Egbert Tannich, Iris Bruchhaus   +2 more
exaly   +2 more sources

Crystal Structure of Glycyl Endopeptidase from Carica papaya: A Cysteine Endopeptidase of Unusual Substrate Specificity

Biochemistry, 1995
Glycyl endopeptidase is a cysteine endopeptidase of the papain family, characterized by specificity for cleavage C-terminal to glycyl residues only and by resistance to inhibition by members of the cystatin family of cysteine proteinase inhibitors. Glycyl endopeptidase has been crystallized from high salt with a substrate-like inhibitor covalently ...
O'Hara, Bernard P., Hemmings, Andrew M., Buttle, David J., Pearl, Laurence H.   +3 more
openaire   +3 more sources

Chinese hamster ovary cells continuously secrete a cysteine endopeptidase

In Vitro Cellular & Developmental Biology, 1990
The protease activity in serum-free conditioned medium of chinese hamster ovary (CHO) cells was measured using peptidyl (or aminoacyl)-4-methylcoumaryl-7-amides (MCAs) as the substrates. Aminopeptidase increased in level as amounts of nonviable cells increased during cultivation in serum-free medium, indicating that the activity seems to be originated ...
M, Satoh, S, Hosoi, S, Sato
openaire   +2 more sources

Toward Computer-Based Cleavage Site Prediction of Cysteine Endopeptidases

Biological Chemistry, 2003
Identification of relevant substrates is essential for elucidation of in vivo functions of peptidases. The recent availability of the complete genome sequences of many eukaryotic organisms holds the promise of identifying specific peptidase substrates by systematic proteome analyses in combination with computer-based screening of genome databases ...
Lohmüller, T., Wenzler, D., Hagemann, Sascha, Kiess, Wieland, Peters, Christoph, Dandekar, Thomas, Reinheckel, Thomas   +6 more
openaire   +3 more sources

A high-molecular-weight cysteine endopeptidase from rat skeletal muscle

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
A cytosolic enzyme of high molecular weight (about 500 000), which attacks native or denatured proteins (inter alia, casein, globin and hexokinase) was purified about 1000-fold from mixed rat skeletal muscles, including muscles freed of mast cells by prior treatment of the animals with the degranulator, compound 48/80.
F, Ismail, W, Gevers
openaire   +2 more sources