Stability and storage conditions of NADH-cytochrome b5 reductase cross-linked into gelatin by chromium (III) acetate

Biomaterials. 1994 Jun;15(8):587-92. doi: 10.1016/0142-9612(94)90208-9.

Abstract

NADH-cytochrome b5 reductase was isolated and partially purified from rabbit liver microsomes. It was immobilized into gelatin by chemical cross-linking. Chromium (III) acetate was used as cross-linker. The effects of pH and temperature on the immobilized cytochrome b5 reductase were investigated. The reusability and storage stability of immobilized enzyme were also tested. Immobilized NADH-cytochrome b5 reductase activities were found to be stable for at least 72 d and 24 uses. The storage stability of NADH-cytochrome b5 reductase was improved with immobilization at 25 degrees C.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates*
  • Acetic Acid
  • Animals
  • Cross-Linking Reagents
  • Cytochrome Reductases / chemistry*
  • Cytochrome Reductases / isolation & purification
  • Cytochrome-B(5) Reductase
  • Drug Storage
  • Enzyme Stability
  • Enzymes, Immobilized
  • Gelatin
  • Hydrogen-Ion Concentration
  • Microsomes, Liver
  • Rabbits
  • Temperature

Substances

  • Acetates
  • Cross-Linking Reagents
  • Enzymes, Immobilized
  • Gelatin
  • Cytochrome Reductases
  • Cytochrome-B(5) Reductase
  • Acetic Acid