Purification and immunochemical analysis of cytochrome c from Neurospora crassa

Susan Stade; Robert Brambl

doi:10.1016/0147-5975(80)90023-7

Purification and immunochemical analysis of cytochrome c from Neurospora crassa

Susan Stade
, Robert Brambl

Plant and Microbial Biology

Research output: Contribution to journal › Article › peer-review

4 Scopus citations

Abstract

Procedures were refined and improved for the purification of cytochrome c from Neurospora crassa, for development of specific antisera to the protein, and for immunochemical identification of cytochrome c after in vivo synthesis and radiolabeling with ³H and ³⁵Fe. The cytochrome c was obtained in high yields via column chromatography and salt fractionation, and the product was pure as judged by spectrophotometric and electrophoretic criteria. Effective, specific antisera to cytochrome c could be obtained only after the monomeric protein antigen was crosslinked with glutaraldehyde; immunoprecipitation of cytochrome c synthesized in vivo was achieved efficiently with a double-antibody procedure.

Original language	English (US)
Pages (from-to)	186-190
Number of pages	5
Journal	Experimental Mycology
Volume	4
Issue number	2
DOIs	https://doi.org/10.1016/0147-5975(80)90023-7
State	Published - Jun 1980

Bibliographical note

Funding Information:
This research was supported by NIH Research Grant GM-19398 from the National Institute of General Medical Sciences.

Keywords

Neurospora crassa
cytochrome c, immunochemical identification, purification
double-antibody procedure

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10.1016/0147-5975(80)90023-7

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title = "Purification and immunochemical analysis of cytochrome c from Neurospora crassa",

abstract = "Procedures were refined and improved for the purification of cytochrome c from Neurospora crassa, for development of specific antisera to the protein, and for immunochemical identification of cytochrome c after in vivo synthesis and radiolabeling with 3H and 35Fe. The cytochrome c was obtained in high yields via column chromatography and salt fractionation, and the product was pure as judged by spectrophotometric and electrophoretic criteria. Effective, specific antisera to cytochrome c could be obtained only after the monomeric protein antigen was crosslinked with glutaraldehyde; immunoprecipitation of cytochrome c synthesized in vivo was achieved efficiently with a double-antibody procedure.",

keywords = "Neurospora crassa, cytochrome c, immunochemical identification, purification, double-antibody procedure",

author = "Susan Stade and Robert Brambl",

note = "Funding Information: This research was supported by NIH Research Grant GM-19398 from the National Institute of General Medical Sciences.",

year = "1980",

month = jun,

doi = "10.1016/0147-5975(80)90023-7",

language = "English (US)",

volume = "4",

pages = "186--190",

journal = "Experimental Mycology",

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publisher = "Academic Press Inc.",

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TY - JOUR

T1 - Purification and immunochemical analysis of cytochrome c from Neurospora crassa

AU - Stade, Susan

AU - Brambl, Robert

N1 - Funding Information: This research was supported by NIH Research Grant GM-19398 from the National Institute of General Medical Sciences.

PY - 1980/6

Y1 - 1980/6

N2 - Procedures were refined and improved for the purification of cytochrome c from Neurospora crassa, for development of specific antisera to the protein, and for immunochemical identification of cytochrome c after in vivo synthesis and radiolabeling with 3H and 35Fe. The cytochrome c was obtained in high yields via column chromatography and salt fractionation, and the product was pure as judged by spectrophotometric and electrophoretic criteria. Effective, specific antisera to cytochrome c could be obtained only after the monomeric protein antigen was crosslinked with glutaraldehyde; immunoprecipitation of cytochrome c synthesized in vivo was achieved efficiently with a double-antibody procedure.

AB - Procedures were refined and improved for the purification of cytochrome c from Neurospora crassa, for development of specific antisera to the protein, and for immunochemical identification of cytochrome c after in vivo synthesis and radiolabeling with 3H and 35Fe. The cytochrome c was obtained in high yields via column chromatography and salt fractionation, and the product was pure as judged by spectrophotometric and electrophoretic criteria. Effective, specific antisera to cytochrome c could be obtained only after the monomeric protein antigen was crosslinked with glutaraldehyde; immunoprecipitation of cytochrome c synthesized in vivo was achieved efficiently with a double-antibody procedure.

KW - Neurospora crassa

KW - cytochrome c, immunochemical identification, purification

KW - double-antibody procedure

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UR - https://www.scopus.com/pages/publications/0019121399#tab=citedBy

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DO - 10.1016/0147-5975(80)90023-7

M3 - Article

AN - SCOPUS:0019121399

SN - 0147-5975

VL - 4

SP - 186

EP - 190

JO - Experimental Mycology

JF - Experimental Mycology

IS - 2

ER -

Purification and immunochemical analysis of cytochrome c from Neurospora crassa

Abstract

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