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Purification of cytochrome b5 from pig testis microsomes by isoelectric focusing in an immobiline pH gradient.
Protein Expr Purif. 1998 Apr; 12(3):420-4.PE

Abstract

Testicular cytochrome b5 was purified by a procedure including preparative isoelectrofocusing. The cytochrome b5 was determined to have an isoelectric point of 4.45 on analytical isoelectric focusing. The purified cytochrome b5 was found to be homogeneous and its molecular weight was estimated to be 16,000 on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The oxidized and reduced forms of the purified preparation exhibited absorption spectra of a typical cytochrome b5. A 69-fold purification was achieved with an overall yield of 6.2%. Following preparation of the microsomes, the purification is accomplished by a two-step procedure utilizing column chromatography and preparative isoelectric focusing.

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Authors+Show Affiliations

Kuwada M
School of Medicine, School of Medicine, Kitasato University, 1-15-1 Kitasato, Sagamihara, Kanagawa, 228, Japan.
Hasumi H
No affiliation info available
Furuse Y
No affiliation info available

MeSH

AcrylamidesAnimalsCytochromes b5Electrophoresis, Polyacrylamide GelHydrogen-Ion ConcentrationIsoelectric FocusingMaleMicrosomesSwineTestis

Pub Type(s)

Comparative Study
Journal Article

Language

eng

PubMed ID

9535711

Citation

Kuwada, M, et al. "Purification of Cytochrome B5 From Pig Testis Microsomes By Isoelectric Focusing in an Immobiline pH Gradient." Protein Expression and Purification, vol. 12, no. 3, 1998, pp. 420-4.
Kuwada M, Hasumi H, Furuse Y. Purification of cytochrome b5 from pig testis microsomes by isoelectric focusing in an immobiline pH gradient. Protein Expr Purif. 1998;12(3):420-4.
Kuwada, M., Hasumi, H., & Furuse, Y. (1998). Purification of cytochrome b5 from pig testis microsomes by isoelectric focusing in an immobiline pH gradient. Protein Expression and Purification, 12(3), 420-4.
Kuwada M, Hasumi H, Furuse Y. Purification of Cytochrome B5 From Pig Testis Microsomes By Isoelectric Focusing in an Immobiline pH Gradient. Protein Expr Purif. 1998;12(3):420-4. PubMed PMID: 9535711.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Purification of cytochrome b5 from pig testis microsomes by isoelectric focusing in an immobiline pH gradient. AU - Kuwada,M, AU - Hasumi,H, AU - Furuse,Y, PY - 1998/5/16/pubmed PY - 1998/5/16/medline PY - 1998/5/16/entrez SP - 420 EP - 4 JF - Protein expression and purification JO - Protein Expr Purif VL - 12 IS - 3 N2 - Testicular cytochrome b5 was purified by a procedure including preparative isoelectrofocusing. The cytochrome b5 was determined to have an isoelectric point of 4.45 on analytical isoelectric focusing. The purified cytochrome b5 was found to be homogeneous and its molecular weight was estimated to be 16,000 on polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The oxidized and reduced forms of the purified preparation exhibited absorption spectra of a typical cytochrome b5. A 69-fold purification was achieved with an overall yield of 6.2%. Following preparation of the microsomes, the purification is accomplished by a two-step procedure utilizing column chromatography and preparative isoelectric focusing. SN - 1046-5928 UR - https://www.unboundmedicine.com/medline/citation/9535711/Purification_of_cytochrome_b5_from_pig_testis_microsomes_by_isoelectric_focusing_in_an_immobiline_pH_gradient_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S1046-5928(97)90849-4 DB - PRIME DP - Unbound Medicine ER -