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Serine protease inhibitor protein inhibitors

Serine protease inhibitor proteins from plants... [Pg.597]

Plant Kunitz serine protease inhibitor proteins... [Pg.602]

Table 12. Plant Kunitz serine protease inhibitor proteins For details see the legend to Table 4. Table 12. Plant Kunitz serine protease inhibitor proteins For details see the legend to Table 4.
Cl-Inh belongs to a superfamily of serine protease inhibitors (serpins) and is a major inhibitor of F-XIIa and kallikrein. It is also an inhibitor of activated complement factors C1 q, C1 r, and C1 s. C1 -Inh thus regulates the activation of two important plasma cascade systems. Proteases induce a conformational change in the plasma protein a2-M, which results in entrapment of the protease into the a2-M cage (B4). In vivo, a2-M acts as a second inhibitor of kallikrein. [Pg.78]

The conformational plasticity supported by mobile regions within native proteins, partially denatured protein states such as molten globules, and natively unfolded proteins underlies many of the conformational (protein misfolding) diseases (Carrell and Lomas, 1997 Dobson et al., 2001). Many of these diseases involve amyloid fibril formation, as in amyloidosis from mutant human lysozymes, neurodegenerative diseases such as Parkinson s and Alzheimer s due to the hbrillogenic propensities of a -synuclein and tau, and the prion encephalopathies such as scrapie, BSE, and new variant Creutzfeldt-Jacob disease (CJD) where amyloid fibril formation is triggered by exposure to the amyloid form of the prion protein. In addition, aggregation of serine protease inhibitors such as a j-antitrypsin is responsible for diseases such as emphysema and cirrhosis. [Pg.105]

Based on the mixed-phase method, ACE is introduced for studying the interaction of heparin with the serine protease inhibitors, antithrombin III (ATIII) and secretory leukocyte proteinase inhibitor (SLPI) (85). An etched capillary, to which heparin has been covalently immobilized, was used in this study. This modified capillary both afforded an improvement in the separation of heparin-binding proteins and required a lower quantity of loaded protein. [Pg.301]


See other pages where Serine protease inhibitor protein inhibitors is mentioned: [Pg.450]    [Pg.607]    [Pg.609]    [Pg.51]    [Pg.560]    [Pg.607]    [Pg.609]    [Pg.34]    [Pg.589]    [Pg.315]    [Pg.353]    [Pg.414]    [Pg.274]    [Pg.93]    [Pg.279]    [Pg.269]    [Pg.376]    [Pg.364]    [Pg.168]    [Pg.276]   
See also in sourсe #XX -- [ Pg.617 ]

See also in sourсe #XX -- [ Pg.617 ]




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Bowman-Birk serine protease inhibitor proteins

Non-protein serine protease inhibitor from natural sources

Non-protein serine protease inhibitor phenolics

Non-protein serine protease inhibitor terpenes

Plant Kunitz serine protease inhibitor proteins

Protease inhibitors proteins

Protein inhibitor

Proteins Serine

Proteins proteases

Proteins serine protease

Serin proteases

Serine inhibitor

Serine protease

Serine protease inhibitor

Serine protease inhibitor proteins

Serine protease inhibitor proteins

Serine proteases protease inhibitors

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