Formation of Zinc Protoporphyrin IX form Myoglobin with Pork Loin Extract

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The formation of zinc protoporphyrin ⅠⅩ (ZPP) with pork loin extract was determined by visible absorption and fluorecsent spectral analyses. After the aaerobic incubation ( in the dark at pH 5.5 and 30℃) of the extract with metmyoglobrin and ZnCl2, characteristic peaks in absorption and spectra were observed at 417,546, and 584 nm. In fluorescent spectrs, a peak was observed at 589nm. Formed amounts of ZPP estimated from the fluorescent intensity at 589 nm was 15.5 nmol/mL-pork extract. The difference in the formations was significantly facilitated by the use of ATP. Zin chelatase activity of loin extract was assayed with protoporphyrin ⅠⅩ and it was estimated as 42mU/mL-extract. The Fe-Zn substituting activity of the extract was assayed with myoglobrin as a substrate. Under the asasy conditions at pH5.5 and 40℃, ZPP was maekedly increased with increasing time by using oxymyoglobrin reduced with ascorbate, white little increase was observed with metmyoglobrin. The activity was estimated as 4.1mU/mL-extract with oxymyoglobrin. At pH5.5-7.0, higher activities were observed as lower pH.
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