Results 261 to 270 of about 778,605 (292)
Some of the next articles are maybe not open access.
Folding studies of the cysteine proteinase inhibitor — human stefin A
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991Reversible GuHCl denaturation of human stefin A (25 degrees C, pH 8) was monitored by the tyrosine fluorescence, by circular dichroism in the near UV and by circular dichroism in the far UV. In each case a midpoint of 2.8 +/- 0.1 M GuHCl was obtained, demonstrating the cooperativity of the denaturation.
E, Zerovnik +3 more
openaire +2 more sources
Interaction of the cysteine proteinase inhibitor chicken cystatin with papain
Biochemistry, 1988The two forms of chicken cystatin, with different isoelectric points, that have been described previously were indistinguishable in analyses of amino- and carboxy-terminal residues, amino acid composition, and peptide maps. The two forms thus are highly similar and most likely differ only in an amide group or in a small charged substituent. The binding
P, Lindahl +3 more
openaire +2 more sources
Acid Cysteine Proteinase Inhibitor in Cutaneous Lymphocytic Infiltrates
The American Journal of Dermatopathology, 1995Acid cysteine proteinase inhibitor (ACPI, cystatin A) is normally present in squamous epithelium and dendritic cells of lymphoid follicles. Its expression is altered both in proliferative and malignant squamous epithelium and in neoplastic lymphoid follicles.
H J, Aho +5 more
openaire +2 more sources
A cysteine proteinase inhibitor purified from apple fruit
Phytochemistry, 1998A cysteine proteinase inhibitor has been purified from immature fruit of Malus domestica (var. Royal Gala). The M(r) of this apple cystatin is estimated to be 10,700 by MALDI-TOF mass spectrometry, 11 300 by SDS-PAGE and 11,000 by gel filtration. It is a relatively strong inhibitor of papain with a Ki value of 0.21 nM and also inhibits ficin and ...
S N, Ryan, W A, Laing, M T, McManus
openaire +2 more sources
Inhibitors of cysteine proteinases from potato.
Biological chemistry Hoppe-Seyler, 1989Potato tubers contain considerable amounts of inhibitors of cysteine proteinases. The majority of inhibitory activity is due to low-molecular mass inhibitors differing in isoelectric points. Three of them were obtained in homogenous form, namely PCPIs (potato cysteine proteinase inhibitors) 6.6 (Mr 25,000), 8.3 and 9.4 (both Mr 22,000).
J, Brzin +4 more
openaire +1 more source
A lysosomotropic polymeric inhibitor of cysteine proteinases
Journal of Controlled Release, 1986V. Šubr +4 more
openaire +1 more source
Human cysteine proteinase inhibitors
Scandinavian Journal of Clinical and Laboratory Investigation, 1988openaire +1 more source