The enzymatic degradation of chondroitin sulfuric acid can be catalyzed by purified bovine testicular hyaluronidase (1, 2) and by an enzyme preparation from Flavobacterium heparinum (3). Dodgson and Lloyd (4) obtained a chondroitinase from Proteus vulgaris that converted chondroitin sulfuric acid to the disaccharide, N-acetylchondrosin sulfate. Previous work from this laboratory (5) has confirm...

Horseshoe crabs (Limulus polyphemus and Tachypleus tridentatus) possess a proteolytic blood coagulation system within their amebocytes that, after release and endotoxin activation, generates a polymerized insoluble coagulin clot. Clotting enzyme from horseshoe crab amebocyte lysate is the protease that activates the clottable protein (coagulogen) which then forms the coagulin clot. Comparison o...

An enzyme, “protein methylase I,” which methylates its endogenous protein has been purified from calf thymus. Acid hydrolysis of the methylated endogenous protein gives rise to two methylated amino acid derivatives. Both derivatives are very sensitive to alkali treatment, and one of the decomposition products is identified as methylurea. These findings, as well as other evidence, indicate that ...

Purification of cyclic 3’,5’-nucleotide phosphodiesterase of bovine brain cerebrum resulted in partial loss of activity, due to dissociation of an activator (or cofactor) from the enzyme. A systematic study showed that as purification proceeded, the activator was removed from phosphodiesterase in a stepwise fashion. Fractions representing phosphodiesterase at different stages of purification co...

The purification of proteins by conventional procedures is frequently laborious and incomplete, and the yields are often low. Enzyme isolation based on a highly specific biological property-strong reversible association with specific substrates or inhibitors-has received only limited attention.‘-’ In affinity chromatography, the enzyme to be purified is passed through a column containing a cros...

A procedure for the purification of the enzyme NADPH:protochlorophyllide oxidoreductase is described. This involves fractionation of sonicated oat etioplast membranes by discontinuous-sucrose-density-gradient centrifugation, which gives membranes in which the enzyme is present at a high specific activity. The enzyme is solubilized from the membranes with Triton X-100, followed by gel filtration...

The citrate-condensing enzyme was isolated as a crystalline protein from pig heart by Ochoa et al. (1). These workers reported that pig heart contained considerable quantities of the condensing enzyme. We were surprised when we obtained much higher yields of this enzyme from pig heart tissue with a different extraction procedure (2). This observation led to a purification procedure that yields ...