Evidence that two forms of bovine erythrocyte cytochrome b5 are identical to segments of microsomal cytochrome b5.

Douglas, R.; Hultquist, Donald E.

doi:10.1073/pnas.75.7.3118

Cited by 18 publications

(12 citation statements)

References 22 publications

(19 reference statements)

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“…4 shows the DEAE-cellulose elution profile for a preparation of soluble cytochrome b5 derived from 4.5 ml of packed erythrocytes from mouse blood. The oxidized, reduced, and reduced minus oxidized spectra are similar to the spectra of soluble cytochrome b5 from human, bovine, and rabbit erythrocytes (6,31). The reduced minus oxidized difference spectrum (Fig .…”

Section: Cytosolic Cytochrome B 5: Its Presence In Mouse Erythrocytesmentioning

confidence: 55%

Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cell.

Slaughter¹,

Hultquist²

1979

The Journal of Cell Biology

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We have obtained and studied a 105,000-g pellet from T-3-C1-2 cells, a cloned line of Friend virus-induced erythroleukemia cells. By difference spectrophotometry, the pellet was shown to contain cytochrome b5 and cytochrome P-450, In the present study, we have used the Friend virus-induced erythroleukemia T-3-C1-2 line as a model for early erythroid cells to study cytochrome b5 , a protein found in reticulocytes and mature erythrocytes . In non-nucleated erythroid cells, cytochrome b5 (16, 31) and cytochrome b5 reductase (16,20,30,39) exist in the cytoplasm as soluble molecules . Erythrocyte cytochrome 65 is similar to cytochrome b5 solubilized from microsomes of the liver. The amino acid composition of bovine erythrocyte cytochrome b5 I is in very good agreement with a segment (residues 1-97) of bovine liver microsomal cytochrome b5 (6) . Tryptic digestions It is our contention that, in the immature erythroid cell, cytochrome b5 is associated with membranes, and that sometime during the maturation process this hydrophobic membrane-bound protein is converted to a water-soluble molecule . In this paper we will present evidence that cytochrome b5 in an immature erythroid cell system exists as a membrane-bound protein. Some of these results have been presented previously in abstract form (36) .

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Section: Cytosolic Cytochrome B 5: Its Presence In Mouse Erythrocytesmentioning

confidence: 55%

Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cell.

Slaughter¹,

Hultquist²

1979

The Journal of Cell Biology

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“…Recent evidence suggests that erythrocyte cytochrome bs is converted from a membrane-bound form to a soluble protein by proteolytic activity which cleaves off a 95 amino acid peptide that apparently seems to anchor the hemoprotein to the membrane [8].…”

Section: Discussionmentioning

confidence: 99%

Proteolytic degradation of human erythrocyte band 3 by membrane-associated protease activity

et al. 1979

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Antisera directed against the cytoplasmic portion of human erythrocyte Band 3 were used to follow the degradation of the band 3 molecule. Small amounts of Band 3 were degraded when well-washed red cell membrane ghosts were incubated in the cold; this process was greatly accelerated by incubating ghosts were incubated in the cold; this process was greatly accelerated by incubating ghosts at 37 degrees C. Band 3 labeled with pyridoxal-phosphate was digested at comparable rates. Band 3 digestion also took place when alkali-extracted ghost membranes were incubated at 37 degrees for prolonged periods. These results suggest that human erythrocytes contain tightly bound, membrane-associated proteolytic activity.

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“…115, No. 3,1983 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Cytochrome b 5 was isolated from the hemolysate by anion exchange chromatography on DE-52 cellulose.…”

Section: E~perimi~al Merhodsmentioning

confidence: 99%

Purification and structural studies of rabbit erythrocyte cytochrome b5

Schafer¹,

Hultquist²

1983

Biochemical and Biophysical Research Communications

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A single form of cytochrome b5 has been isolated in highly purified form from the cytosolic fraction of rabbit erythrocytes by sequential chromatography on DE-52 cellulose, Sephadex G-75, and DEAE-Sephadex A50. The cytochrome is structurally similar to the N-terminal, heme-binding domain of rabbit liver microsomal cytochrome b5. Like the liver protein, it is blocked at the amino terminus. Its amino acid composition is similar to that of residues 1-97 of the microsomal protein. With one exception, tryptic peptides derived from apo-cytochrome b5 of rabbit erythrocytes co-elute with the tryptic peptides obtained from a soluble hemepeptide fragment of microsomal cytochrome b5. These findings, together with amino acid sequence analysis of the carboxyl terminal tryptic peptides, identify the erythrocyte cytochrome b5 as a 97-residue peptide.

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Evidence that two forms of bovine erythrocyte cytochrome b5 are identical to segments of microsomal cytochrome b5.

Cited by 18 publications

References 22 publications

Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cell.

Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cell.

Proteolytic degradation of human erythrocyte band 3 by membrane-associated protease activity

Purification and structural studies of rabbit erythrocyte cytochrome b5

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