Download A New Model for Analyzing Antimicrobial Peptides With by E.L. Cooper, A. Beschin, M. Bilej (editors) PDF

By E.L. Cooper, A. Beschin, M. Bilej (editors)

This quantity first offers facts for the earthworm's immune process; the implications strongly recommend that yes molecules of the earthworm's immune process will be exploited as common antibiotics - hence the biomedical purposes. Earthworms have a powerful immune procedure due to the fact melanoma can't be precipitated in them, nor does it appear to take place in traditional populations. Cytoxicity of melanoma cells has been tested in terms of earthworm leukocytes dependent upon: constitution; phone differentiation antigens; and serve as published by means of FACS and mAbs.

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Additional info for A New Model for Analyzing Antimicrobial Peptides With Biomedical Applications (Nato: Life and Behavioural Sciences, 343)

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The stability of immobilized lumbrokinase was determined by caseinolytic activity assay and the specificity of immobilized lumbrokinase on fibrinogen/fibrin was observed by SDS-PAGE. Immobilized lumbrokinase retained about 34 % of its activity, when compared to its soluble state and it also demonstrated stability against thermal inactivation and degradation and within a pH range. 0 pH unit upward when compared with the soluble enzyme. Immobilized lumbrokinase demonstrated stable proteolytic activity during various incubation periods in addition to proteolyzing fibrinogen and fibrin almost specifically, while hardly hydrolyzing other plasma proteins including plasminogen and albumin.

Analyses of substrate specificity and inhibition indicated that these enzymes were trypsin-like serine proteases. The N-terminal amino acid sequences of the enzymes revealed similarities to those of trypsin-like enzymes such as elastase and coagulation factor IX. These six enzyme proteins were suggested to derive as isozyme(s) from at least four different genes. The strongest fibrinolytic protease of the six enzyme proteins purified from Lumbricus rubellus (F-III-2) have been modified chemically with fragmented human serum albumin (1030 kDa)[68].

Immobilized lumbrokinase retained about 34 % of its activity, when compared to its soluble state and it also demonstrated stability against thermal inactivation and degradation and within a pH range. 0 pH unit upward when compared with the soluble enzyme. Immobilized lumbrokinase demonstrated stable proteolytic activity during various incubation periods in addition to proteolyzing fibrinogen and fibrin almost specifically, while hardly hydrolyzing other plasma proteins including plasminogen and albumin.

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