A fucoidan extracted from Saccharina japonica was fractionated by anion exchange chromatography. The most complex fraction F0.5 was degraded by dilute sulphuric acid and then separated by use of an activated carbon column. Fraction Y1 was fractionated by anion exchange and gel filtration chromatography while Fraction Y2 was fractionated by gel filtration chromatography. The fractions were deter...

Embryotrophic factors from human oviductal cells were partially purified by liquid chromatographic methods. The conditioned medium from human oviductal cell culture was fractionated successively by concanavalin A (Con-A) affinity chromatography, ion-exchange chromatography and gel filtration. The presence of the embryotrophic activity in the eluates was determined by the stimulatory effects on ...

Edestin, a major hempseed storage protein from Cheungsam, was isolated to apparent homogeneity by acid precipitation and gel filtration chromatography. The native molecular weight of purified edestin was approximately 300 kDa by Sephacryl S-300 gel filtration. Upon adding 2mercaptoethanol, the isolated edestin of 56.7 kDa on the non-reduced sodium dodecyl sulfate polyacrylamide gel was converte...

When proacrosin from mouse epididymal spermatozoa was activated a single form of acrosin was produced. The enzyme was isolated by gel filtration followed by affinity chromatography using Sepharose-4B linked to an acrosin inhibitor p-(p'-aminophenoxypropoxy)benzamidine. The molecular weight of partly purified acrosin was 53 000 by gel filtration, and of the pure enzyme 39 000 by SDS-polyacrylami...

An inhibitor of mammalian collagenase from bovine scapular cartilage has been purified to homogeneity. The inhibitor, extracted from cartilage using 2 M NaCl, was applied to an A-1.5m gel filtration column. Inhibitor eluted at an apparent Mr of 28,000. Further purification was achieved by ion exchange chromatography, gel filtration, and reverse-phase high performance liquid chromatography. A pu...

Arylsulfatase A (cerebroside sulfate sulfohydrolase) was purified 3500-fold at a 7% yield from human urine. A crude urinary protein concentrate was prepared by treating pooled urine with ammonium sulfate and subsequently drying the precipitate with acetone. The powder thus obtained was extracted with buffer and was subjected to chromatographic and electrophoretic procedures as follows: (a) ammo...