Results 31 to 40 of about 70 (65)

Bullfrog plasma cysteine proteinase inhibitor (CPI)

Immunopharmacology, 1996
Papain is inhibited by bullfrog plasma. CPI was isolated from bullfrog plasma by two step column chromatography; Cm-papain agarose column chromatography followed by FPLC Mono Q column chromatography with addition of benzamidine. Isolated CPI gave a single band on SDS-PAGE under reducing condition, and the molecular weight of reduced CPI was estimated ...
H, Mashiko, H, Takahashi
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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
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Cysteine proteinase inhibitors produced by mononuclear phagocytes

Cell and Tissue Research, 1984
Monocytes were separated from human peripheral blood and allowed to attach to culture flasks, after which the content and production of a number of cysteine proteinase inhibitors was assayed. These were: a low molecular weight (MW 12000) acid cysteine proteinase inhibitor (ACPI); a low-molecular weight inhibitor of the same size with neutral pH (NCPI),
V K, Hopsu-Havu, I A, Joronen, M, Järvinen, A, Rinne, M, Aalto   +4 more
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Caiman Kininogen-Like Cysteine Proteinase Inhibitor

1992
Kininogens are the major mammalian plasma cysteine proteinase inhibitors; a kininogen-like protein was also found in the snake Bothrops jararaca plasma. This communication describes a kininogen-like protein in plasma of Caiman crocodilus vacare. Caiman crude plasma, unlike snake plasma, contains a detectable cysteine proteinase inhibitor. The inhibitor
M S, Araujo, R, Andreotti, A M, Chudzinski, C A, Sampaio, M U, Sampaio   +4 more
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Assay of α-Cysteine Proteinase Inhibitor in Serum or Plasma

Hoppe-Seyler´s Zeitschrift für physiologische Chemie, 1982
A new proteinase inhibitor has recently been found in human serum or plasma which specifically inhibits cysteine proteinases such as ficin, papain, bromelain and cathepsin B. However, serum contains alpha 2-macroglobulin which also inhibits these cysteine proteinases and, consequently, interferes with the assay of the new alpha-cysteine proteinase ...
K, Minakata, M, Asano, T, Sato, N, Harada   +3 more
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Serum α-cysteine proteinase inhibitor levels in pregnancy

Clinical Biochemistry, 1983
Variation in alpha-cysteine proteinase inhibitor levels in human sera were investigated with special attention to the effect of pregnancy and diseases. The inhibitor level in 111 pregnant women, examined by our previous method, increased as the pregnancy advanced.
K, Minakata, M, Asano, H, Mizutani, Y, Kawashima   +3 more
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Cysteine proteinase inhibitors from rabbit skeletal muscle

International Journal of Biochemistry, 1988
1. Two cysteine proteinase inhibitors, I-T (Mr = 29,000) and I-S (Mr = 10,700), were isolated from rabbit skeletal muscle by means of succesive extraction with a neutral buffer solution, precipitation at pH 3.7, acetone fractionation and gel permeation on Sephadex G-75. 2.
M, Matsuishi, A, Okitani, Y, Hayakawa, H, Kato   +3 more
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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
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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
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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
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