منابع مشابه
In situ localization and substrate specificity of earthworm protease-II and protease-III-1 from Eisenia fetida.
Recently, the function in fibrinolysis of earthworm proteases has been studied. In our experiments, earthworm protease-II (EfP-II) and earthworm protease-III-1 (EfP-III-1) were isolated and purified from Eisenia fetida. As shown by the assay of sections of the earthworm on fibrin plates, the enzymic activity was mainly detected around the clitellum. In the presence of anti-EfP-II or anti-EfP-II...
متن کاملFurther stabilization of earthworm serine protease by chemical modification and immobilization.
Earthworm serine protease is more stable and is less affected by organic solvents and detergent than other proteases. However, it is inactivated, probably by autolysis, at 60 degrees C or above under alkaline conditions. Further stabilization was managed by chemical modification of the enzyme with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide and phenylglyoxal to protect the activity from the a...
متن کاملBrownian Earthworm
We prove that the distance between two reflected Brownian motions outside a sphere in a 3-dimensional flat torus does not converge to 0, a.s., if the radius of the sphere is sufficiently small, relative to the size of the torus.
متن کاملGalvanotropism in the Earthworm
In a former paper Kellogg and the writer have described the effects of a galvanic current on the body positions of Lumbricus Ierres~ris. 1 When the current flows transversely through such an animal or piece of one, the muscles respond by unilateral contraction on the cathodal side. The result is to bring the ends of the worm toward the cathode, thus forming a U with the median part nearest the ...
متن کاملChemical modification of earthworm fibrinolytic enzyme with human serum albumin fragment and characterization of the protease as a therapeutic enzyme.
The strongest fibrinolytic protease (F-III-2) in the six enzyme proteins purified from earthworm, Lumbricus rubellus [N. Nakajima et al., Biosci. Biotech. Biochem., 57, 1726-1730 (1993)] has been modified chemically with fragmented human serum albumin (mol. wt., 10,000-30,000). The modified enzyme lost the antigenicity of the native enzyme and reacted with the antisera against human serum album...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Applied and Environmental Soil Science
سال: 2010
ISSN: 1687-7667,1687-7675
DOI: 10.1155/2010/294258