Papain proteolysis releases a soluble NADPH dependent diaphorase activity from bovine neutrophil membranes. Academic Article

abstract

• An NADPH dependent cytochrome c reductase has been purified from resting bovine neutrophil membranes. A high degree of purification, approaching homogeneity, is indicated by the presence of a single 75 kDa protein band on silver stained SDS-PAGE (10%). The purified protein catalyzes as well an NADPH dependent reduction of iodonitrotetrazolium violet (INT). Limited papain digestion of the purified preparation produces a 65 kDa product which retains both enzymatic activities. In a similar fashion papain digestion of the plasma membrane bound protein generates a fully active soluble NADPH dependent INT and cytochrome c reductase preparation (65 kDa). Proteolytic cleavage would appear to occur at a protein-membrane anchor remote from the proteins catalytic site. The cytochrome c reductase acts independently of the O2-generating cytochrome b558, a leukocyte plasma membrane protein which also catalyzes an NADPH dependent INT reduction.

authors

• Li, Jianrong

published proceedings

• FEBS Lett

author list (cited authors)

• Li, J., Kon, L. M., & Guillory, R. J.

citation count

• 1

complete list of authors

• Li, J||Kon, LM||Guillory, RJ

publication date

• March 1998

publisher

• Wiley  Publisher

published in

• FEBS Letters  Journal

keywords

• Animals
• Cattle
• Cell Membrane
• Cytochrome C Group
• Dihydrolipoamide Dehydrogenase
• Membrane Proteins
• NADP
• Nadh Dehydrogenase
• Neutrophils
• Oxidation-Reduction
• Oxygen
• Papain
• Superoxide Dismutase
• Tetrazolium Salts

PubMed Central ID

• 9539148

Digital Object Identifier (DOI)

• 10.1016/s0014-5793(98)00171-9

start page

• 188

end page

• 192

volume

• 424

issue

• 3

URL

• http://dx.doi.org/10.1016/s0014-5793(98)00171-9