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PMID: 7034720 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Molecular and antigenic properties of cytochrome b5 from slow-muscle sarcoplasmic reticulum.

The Biochemical journal ·Vol. 197 ·No. 2 ·1981-08-01 ·Pages 515-8

Salviati G, Salvatori S, Betto R, Margreth A

Abstract

NADH--cytochrome b5 reductase and cytochrome b5 associated with slow-muscle sarcoplasmic reticulum and liver microsomal fraction were identified with discrete protein bands of molecular weights 33000 and 16700 by polyacrylamide-gel electrophoresis. Purified detergent-extracted cytochrome b5 from muscle sarcoplasmic reticulum is indistinguishable from liver microsomal cytochrome b5 with respect to spectral properties, pI values and immunological reactivity with antibody to the liver cytochrome b5. Reaction of the antibody with membrane-bound cytochrome b5 inhibits the sarcoplasmic-reticulum NADH--cytochrome c reductase activity.

MeSH Terms
Animals Antigens/immunology Cytochrome Reductases/antagonists & inhibitors Cytochrome-B(5) Reductase Cytochromes/immunology Cytochromes b5 Electrophoresis, Polyacrylamide Gel Immunosorbent Techniques Isoelectric Focusing Microsomes, Liver/analysis Muscles/analysis Rabbits Sarcoplasmic Reticulum/analysis
Chemicals
Antigens Cytochromes Cytochromes b5 Cytochrome Reductases Cytochrome-B(5) Reductase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Salviati G
Salvatori S
Betto R
Margreth A
References (15)
15 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1981-08-01
Pages
515-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1163154
Subset
IM
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