| pubmed-article:7146594 | pubmed:abstractText | The possible presence of a glycolytic multienzyme complex in the digestive gland from the mussel, Mytilus galloprovincialis, Lamarck, has been investigated. The digestive gland homogenate was concentrated an applied to a Sepharose-2B column. The elution profile demonstrates that two species of glycolytic enzymes were eluted from the column. Most of the enzyme activity appeared in the low-molecular-weight region, the enzymes being eluted as individual entities in order of their molecular weights. However, a proportion of each enzyme activity was found in the high-molecular-weight region of eluate, with those activities showing a high degree of co-chromatography. By using a column calibrated with a series of marker proteins of known molecular weight, the activity peak for the high-molecular-weight species corresponded to a molecular weight of 3 X 10(6) +/- 10(5) d. Finally, it has been found that a sample of the high-molecular-weight species was able to catalyse the production of piruvate when it was incubated with different glycolytic substrates and the appropriate cofactors. | lld:pubmed |
