Results 331 to 340 of about 108,777 (376)

Cystatin S: A Cysteine Proteinase Inhibitor of Human Saliva

The Journal of Biochemistry, 1984
An acidic protein of human saliva, which we named SAP-1 previously, is now shown to be an inhibitor of several cysteine proteinases. The protein inhibited papain and ficin strongly, and stem bromelain and bovine cathepsin C partially. However, it did not inhibit either porcine cathepsin B or clostripain.
S, Isemura, E, Saitoh, S, Ito, M, Isemura, K, Sanada   +4 more
openaire   +2 more sources

Cysteine proteinase inhibitors in elapid and hydrophiid snake venoms

Toxicon, 2002
The ability of elapid and hydrophiid snake venoms to inhibit cathepsin L was tested. All nine species of elapid and three species of hydrophiid snake venoms tested showed inhibition against cathepsin L. All of these venoms tested also showed inhibition against papain as well as against cathepsin L. Among these venoms, two elapid (Laticauda semifasciata
Hiroshi, Mashiko, Hidenobu, Takahashi
openaire   +2 more sources

Invasiveness of Transformed Human Breast Epithelial Cell Lines Is Related to Cathepsin B and Inhibited by Cysteine Proteinase Inhibitors

Biological chemistry, 2003
The activities of the lysosomal cysteine proteinases cathepsin B and L are regulated by their endogenous inhibitors, stefins A and B, and cystatin C, and their imbalance may be associated with increased invasiveness and development of the malignant cell ...
A. Bervar, I. Zajc, N. Sever, N. Katunuma, Bonnie F. Sloane, T. Lah   +5 more
semanticscholar   +1 more source

Peptide Methyl Ketones as Reversible Inhibitors of Cysteine Proteinases

Journal of Enzyme Inhibition, 1989
Peptide methyl ketones represent a new class of reversible, competitive cysteine proteinase inhibitor with little or no effect on serine proteinases. The affinity of the inhibitors to papain (EC 3.4.22.3), cathepsin B (EC 3.4.22.1) and cathepsin L (EC 3.4.22.15) depends on the peptide chain length and on side-chain effects.
D, Brömme, B, Bartels, H, Kirschke, S, Fittkau   +3 more
openaire   +2 more sources

Cysteine proteinase inhibitors and bleomycin-sensitive and -resistant cells

Biochemical Pharmacology, 1991
We have isolated a new human head and neck carcinoma cell line (C-10E) that is highly resistant to BLM (40-fold) when compared to the parental (A-253) cell line. Consonant with BLM resistance in the C-10E cell line, we found that this cell line accumulated 2- to 3-fold less BLM A2 than A-253 cells.
G, Morris, J S, Mistry, J P, Jani, S M, Sebti, J S, Lazo   +4 more
openaire   +2 more sources

Purification and Characterization of a Rice Cysteine Proteinase Inhibitor

Agricultural and Biological Chemistry, 1987
A proteinaceous substance that inhibited the activity of papain (EC 3.4.22.2) was found in seeds of rice, Oryza sativa L. japonica. This cysteine proteinase inhibitor (CPI) was purified by a series of purification procedures including CM-Sephadex C-50, Sephadex G-75, and DEAE- Sephadex A-50 chromatography.
Keiko ABE, Hiroto KONDO, Soichi ARAI
openaire   +1 more source

Natural cysteine proteinase inhibitors reduce lectin induced lymphocyte stimulation

Acta Histochemica, 1986
Lymphocyte stimulation by lectins can be inhibited by several synthetic inhibitors of proteolytic enzymes, notably those of cysteine proteinases. The effects of naturally occurring enzyme inhibitors are less well known. The effect of the neutral low-molecular weight cysteine proteinase inhibitor (NCPI) recently purified from lymph nodes and spleen was ...
V K, Hopsu-Havu, I A, Joronen, A, Rinne, M, Järvinen   +3 more
openaire   +2 more sources

[Cysteine proteinase inhibitors from soy seeds].

Biokhimiia (Moscow, Russia), 1995
Protein inhibitors of cysteine proteinases possessing unusual properties have been found in soya (Glycine max) seeds. One of the inhibitor forms has also been detected in Bowman-Birk inhibitor preparations (both commercial and purified by affinity chromatography on chymotrypsin-Sepharose ones).
A V, Zimacheva, V V, Mosolov
openaire   +1 more source

Inhibitors of cysteine proteinases from potato.

Biological chemistry Hoppe-Seyler, 1989
Potato 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, T, Popović, M, Drobnic-Kosorok, M, Kotnik, V, Turk   +4 more
openaire   +1 more source

Functional characterization of single-domain cystatin-like cysteine proteinase inhibitors expressed by the trematode Fasciola hepatica

Parasitology, 2017
M. Cancela, Ileana Corvo, E. D. da Silva, Aline Teichmann, L. Roche, Á. Díaz, J. Tort, H. Ferreira, A. Zaha   +8 more
semanticscholar   +1 more source