Results 251 to 260 of about 189,208 (289)
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Cysteine proteinase inhibitors in human placenta

Placenta, 1985
When human placental extract was chromatographed on a Sephadex G-75 column, cysteine proteinase inhibitors with molecular weights of 80 000 and 12 300 were eluted. The high molecular weight peak (CPI-H) was identified as alpha-cysteine proteinase inhibitor.
M, Warwas, G, Sawicki
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A Cysteine-Activated Proteinase of Clostridium Histolyticum

The Journal of Immunology, 1952
Discussion and Summary A cysteine-activated proteolytic enzyme present in culture filtrates of Cl. histolyticum has been purified by fractionation in methanol-water mixtures under controlled conditions of pH, ionic strength, protein concentration and temperature and further purified by differential centrifugation, lyophilization and ...
I H, LEPOW   +3 more
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Cysteine proteinase inhibitors in psoriatic epidermis

Archives of Dermatological Research, 1983
Human psoriatic epidermis and scales were demonstrated to contain two antigenically separate cysteine proteinase inhibitors, one acidic with an isoelectric point of 4.7-5.0 (ACPI) and one neutral with an isoelectric point of 6.0-6.5 (NCPI), while normal epidermis contains only ACPI.
V K, Hopsu-Havu   +3 more
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Cysteine Proteinases and their Inhibitors

1986
Cysteine proteinase inhibitors from fish ...
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Lysosomal cysteine proteinases.

Ciba Foundation symposium, 1981
Cathepsin B has so far been the most investigated cysteine (thiol) proteinase of lysosomes. The use of cytosol proteins as substrates has allowed the detection of two new lysosomal cysteine proteinases from rat liver: the endoaminopeptidase cathepsin H and cathepsin L, which splits almost no synthetic substrates but has a more than 10-fold higher ...
H, Kirschke   +5 more
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[Cysteine proteinase and neurodegeneration].

Revista de neurologia, 2000
This is a review of the part played by the cysteine proteases in different physiological and pathological processes.Apoptotic processes have a crucial function in control of the number of cells in multicellular organisms, both during development and throughout life.
J, Jordán   +3 more
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The Characteristics of Cysteine Proteinases of Parasitic Protozoa

Biological Chemistry Hoppe-Seyler, 1992
Cysteine proteinases have now been detected in most of the important species of parasitic protozoa. Characterization of the enzymes and sequence determinations have revealed that the enzymes are related to papain and the mammalian cathepsins. All of the protozoan enzymes analyzed to date are members of the cathepsin L/cathepsin H/papain branch of the ...
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The Function of Propeptide Domains of Cysteine Proteinases

2006
The papain-like cysteine proteinases can be divided into cathepsin L-like and cathepsin B-like enzymes because of the extended proregion of the former ones. We performed a series of mutations (alanine scan) in the prodomain of procathepsin S in order to elucidate the function of this extended domain in the L-like cathepsins.
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Localization of cysteine proteinases and an endogenous cysteine proteinase inhibitor in cultured muscle cells

Biochemical Society Transactions, 1985
J W, Bird   +7 more
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The Cysteine proteinases

Tetrahedron, 1976
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