Results 271 to 280 of about 37,687 (302)

Characterization and Structure of Pineapple Stem Inhibitor of Cysteine Proteinases

Biological Chemistry Hoppe-Seyler, 1992
The complete amino acid sequence of the inhibitor of cysteine proteinases from pineapple stem acetone powder was determined. The inhibitor consists of 52 amino acids and is composed of two polypeptide chains (41 and 11 amino acids) linked via disulphide bonds. It differs from already known sequences in one to four amino acids.
B, Lenarcic, A, Ritonja, B, Turk, I, Dolenc, V, Turk   +4 more
openaire   +2 more sources

Cathepsin D inactivates cysteine proteinase inhibitors cystatins

Biochemical and Biophysical Research Communications, 1988
The formation of inactive complexes in excess molar amounts of human cathepsins H and L with their protein inhibitors human stefin A, human stefin B and chicken cystatin at pH 5.6 has been shown by measurement of enzyme activity coupled with reverse-phase HPLC not to involve covalent cleavage of the inhibitors.
B, Lenarcic, J, Kos, I, Dolenc, P, Lucovnik, I, Krizaj, V, Turk   +5 more
openaire   +2 more sources

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

Azapeptides as Inhibitors and Active Site Titrants for Cysteine Proteinases

Journal of Medicinal Chemistry, 1998
Ester and amide derivatives of alpha-azaglycine (carbazic acid, H2NNHCOOH), alpha-azaalanine, and alpha-azaphenylalanine (i.e., Ac-l-Phe-NHN(R)CO-X, where X = H, CH3, or CH2Ph, respectively) were synthesized and evaluated as inhibitors of the cysteine proteinases papain and cathepsin B.
R, Xing, R P, Hanzlik
openaire   +2 more sources

Molecular Biology of Human Salivary Cysteine Proteinase Inhibitors

Critical Reviews in Oral Biology & Medicine, 1993
The synthesis of human cystatins of family II is controlled by a multigene family having at least 7 members that are localized on chromosome 20, the cystatin gene family. Proteolytic degradation and phosphorylation of the gene products give rise to heterogeneity and multiplicity of cystatins in human saliva.
E, Saitoh, S, Isemura
openaire   +2 more sources

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

Antimalarial effects of vinyl sulfone cysteine proteinase inhibitors

Antimicrobial Agents and Chemotherapy, 1996
We evaluated the antimalarial effects of vinyl sulfone cysteine proteinase inhibitors. A number of vinyl sulfones strongly inhibited falcipain, a Plasmodium falciparum cysteine proteinase that is a critical hemoglobinase. In studies of cultured parasites, nanomolar concentrations of three vinyl sulfones inhibited parasite hemoglobin degradation ...
P J, Rosenthal, J E, Olson, G K, Lee, J T, Palmer, J L, Klaus, D, Rasnick   +5 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

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

Localization of cysteine proteinases and an endogenous cysteine proteinase inhibitor in cultured muscle cells

Biochemical Society Transactions, 1985
J W, Bird, L, Wood, I, Sohar, E, Fekete, R, Colella, G, Yorke, B, Cosentino, F J, Roisen   +7 more
openaire   +2 more sources