Polymerization of 10-hydroxydecanoic acid in benzene with polyethylene glycol-modified lipase

Summary A hydrophobic substrate, 10-hydroxydecanoic acid having two functional groups (–OH and –COOH) in the molecule, was polymerized by ester bond formation with the polyethylene glycol-modified lipase in a transparent benzene solution. The polymer of 10-hydroxydecanoic acid was linearly elongated under a quite mild condition.     

Determination of fragment D-dimer derivatives in serum reactive with antiserum against human fragment D-dimer

A previous study demonstrated the preparation of an antiserum having enough specificity and sensitivity for a radioimmunoassay to determine fragment D-dimer derivatives. Using the antiserum the contents of fragment D-dimer derivatives in the sera of normal subjects and patients were determined. The content in normal subjects was 0.260 +/- 0.07 micrograms/ml (mean +/- SD) an that in patients with elevated levels of FDP ranged from 0.30 to 28 micrograms/ml. The values of fragment D-dimer derivatives and FDP in sera of some patients did not necessarily change in parallel, although there seems to be generally a positive correlation between them.     

Visible fibrinolysis by endothelial cells: Effect of vitamins and sterols

We have succeeded in corroborating the enhancing effect of vitamin A, vitamin C, sitosterol and fucosterol on the fibrinolytic activity of endothelial cells. The assay system consisted of anin situ dissolution of a fibrin layer coated onto a culture dish, over which endothelial cells were grown in a culture medium containing 10 % serum. The dissolution was enhanced by the addition of these vitamins and phytosterols to the culture medium.To whom correspondence should be addressed.     

Chemical modification of lipase with ferromagnetic modifier — A ferromagnetic-modified lipase

Summary A ferromagnetic modifier was prepared by reacting ferrous(Fe²⁺)- and ferric(Fe³⁺)-ions with polyethylene glycol having two carboxyl groups (MW:2000) at pH 8.0–8.5. Lipase fromPseudomonas fragi 22–39B was coupled with the modifier using water-soluble carbodiimide. The modified lipase, which was dispersed into buffered solutions in the size range of 30–70 nm, exerted the hydrolytic activity of 8.0 U/mg. In a magnetic field of 250 Oe, the ferromagnetic-modified lipase was readily recovered from the colloidal solution.     

Modification of batroxobin with activated polyethylene glycol: reduction of binding ability towards anti-batroxobin antibody and retention of defibrinogenation activity in circulation of preimmunized dogs

Amino groups of batroxobin (Bothrops atrox thrombic protease) were modified with 2,4-bis(O-methoxypolyethylene glycol)-6-chloro-s-triazine (activated PEG2). The modified batroxobin had the reduced binding ability towards anti-batroxobin antibody but retained its enzymic activity in vitro and in vivo. Administration of modified batroxobin in which 29% of the total amino groups in the molecule had been modified, to beagle dogs preimmunized with native batroxobin gave rise to a marked reduction of the fibrinogen level in plasma, accompanied with an increased level of fibrinogen (fibrin) degradation products, FDP. On the other hand, no reduction of fibrinogen level was observed when native batroxobin instead of modified batroxobin was injected to immunized dogs.