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Subsite substrate specificity of midgut insect chymotrypsins
(PERGAMON-ELSEVIER SCIENCE LTD, 2008)
Insect chymotrypsins are distinctively sensitive to plant protein inhibitors, suggesting that they differ in subsite architecture and hence in substrate specificities. Purified digestive chymotrypsins from insects of three ...
Characterization, subsite mapping and N-terminal sequence of miliin, a serine-protease isolated from the latex of Euphorbia milii
(Elsevier B.V., 2013-04-01)
Miliin is a serine protease purified from the latex of Euphorbia milii. This work reports the effect of pH and temperature on the catalytic activity of miliin, using fluorescence resonance energy transfer (FRET) substrates. ...
Subsite substrate specificity of midgut insect chymotrypsins
(Elsevier B.V., 2008-06-01)
Insect chymotrypsins are distinctively sensitive to plant protein inhibitors, suggesting that they differ in subsite architecture and hence in substrate specificities. Purified digestive chymotrypsins from insects of three ...
Purification and characterization of a new alkaline serine protease from the thermophilic fungus Myceliophthora sp.
(Elsevier B.V., 2011-11-01)
This work reports the purification of a novel alkaline protease enzyme from a putative new thermophilic fungus Myceliophthora sp. The molecular weight of the enzyme was determined as 28.2 kDa by using MALDI-TOF MS and it ...
S3 to S3 ' subsite specificity of recombinant human cathepsin K and development of selective internally quenched fluorescent substrates
(Portland Press, 2003-08-01)
We have systematically examined the S3 to S3' subsite substrate specificity requirements of cathepsin K using internally quenched fluorescent peptides derived from the lead sequence Abz-KLRFSKQ-EDDnp [where Abz is ...
HORSE URINARY KALLIKREIN .2. EFFECT of SUBSITE INTERACTIONS ON ITS CATALYTIC ACTIVITY
(Walter de Gruyter & Co, 1988-05-01)
Penicillium citrinum UFV1 β-glucosidases: purification, characterization, and application for biomass saccharification
(Springer Verlag (Germany), 2019)
The 3D structure and function of digestive cathepsin L-like proteinases of Tenebrio molitor larval midgut
(PERGAMON-ELSEVIER SCIENCE LTDOXFORD, 2012)
Cathepsin L-like proteinases (CAL) are major digestive proteinases in the beetle Tenebrio molitor. Procathepsin Ls 2 (pCAL2) and 3 (pCAL3) were expressed as recombinant proteins in Escherichia coil, purified and activated ...