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2002

Turkish Journal of Biology

Purification

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Full-Text Articles in Life Sciences

Partial Purification Of Intestinal Triglyceride Lipase From Cyprinion Macrostomus Heckel, 1843 And Effect Of Ph On Enzyme Activity, Naci̇ Değerli̇, M. Ali̇ Akpinar Jan 2002

Partial Purification Of Intestinal Triglyceride Lipase From Cyprinion Macrostomus Heckel, 1843 And Effect Of Ph On Enzyme Activity, Naci̇ Değerli̇, M. Ali̇ Akpinar

Turkish Journal of Biology

Intestinal triglyceride lipase (TG) of Cyprinion macrostomus after precipitation with 30% polyethylene glycol (PEG), was partially purified by hydrophobic interaction chromatography on phenyl sepharose CL-4B, and the effect of pH on this enzyme activity was determined titrimetrically. Intestinal tissue homogenates were precipitated using 30% PEG-8000, and then applied onto a phenyl sepharose CL-4B column for hy-drophobic interaction chromatography. The lipase that bound to this hydrophobic resin and was partially purified by this single step application was then eluted from this resin with taurocholic acid and Triton X-100 elution. This purified enzyme effectively hydrolysed natural olive oil substrate under the experimental …


Purification And Determination Of The Molecular Structure Of Hemolymph Lectin Of Agrotis Segetum (Denis And Schiff.), Nursel Gül, Cevat Ayvali Jan 2002

Purification And Determination Of The Molecular Structure Of Hemolymph Lectin Of Agrotis Segetum (Denis And Schiff.), Nursel Gül, Cevat Ayvali

Turkish Journal of Biology

A soluble lectin was purified from the hemolymph of Agrotis segetum by two methods, via affinity chromatography on a Sepharose-4B column and gel filtration on a Superdex-200 column. Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE) showed a single protein band with a molecular weight of 69,000 in both the presence and absence of 2-Mercaptoethanol. Alternatively, the molecular weight of this lectin was estimated to be 69,000 by gel filtration on Superdex-200. Electron microscopic observation of the purified lectin was reticular in structure and consisted of tandem aligned spherical basic units.