Dietary fish oil enriched in very-long-chain polyunsaturated fatty acid reduces cardiometabolic risk factors and improves retinal function.

Very-long-chain polyunsaturated fatty acids (VLCPUFAs; C24-38) constitute a unique class of PUFA that have important biological roles, but the lack of a suitable dietary source has limited research in this field. We produced an n-3 C24-28-rich VLCPUFA-oil concentrated from fish oil to study its bioavailability and physiological functions in C57BL/6J mice. The serum and retinal C24:5 levels increased significantly compared to control after a single-dose gavage, and VLCPUFAs were incorporated into the liver, brain, and eyes after 8-week supplementation.

Heterogeneity of the Fatty Acid Composition of Japanese Placentae for Determining the Perinatal Fatty Acid Status: a Methodological Study.

Analysis of the placenta can be a useful way to determine the fatty acid (FA) status of pregnant women and neonates since this large organ can be obtained easily and non-invasively. Although several studies have been conducted on using placental tissue for FA analysis, the sampling methods have not been thoroughly examined. The aim of the present study was to determine a suitable method of sampling human placentae by focusing on their heterogeneity.

PEG-inhibitor conjugates: application of diphenyl alpha-aminoalkylphosphonate to removal of chymotrypsin.

Diphenyl 1-amino-2-phenylethylphosphonate was introduced to poly(ethylene glycol)s (PEGs) with average molecular masses of 300, 400, and 600 to prepare water-insoluble PEG-inhibitor conjugates. Interestingly, only the conjugate from PEG with an average molecular weight of 600 formed a precipitate with chymotrypsin but not with trypsin. The results demonstrated that the PEG-inhibitor conjugate is useful for separation of chymotrypsin.

Selective removal of chymotrypsin using diphenyl alpha-aminoalkylphosphonate immobilized on sepharose gel.

A diphenyl alpha-aminoalkylphosphonate derivative, which is an irreversible inhibitor of chymotrypsin-like serine proteases, was immobilized on cyanogen bromide-activated Sepharose, and the selective binding of chymotrypsin to the obtained inhibitor-gel was evaluated using batch and column methods. Complete removal of chymotrypsin in an aqueous solution was done using the column method, while partial removal was done using the batch method.