Peroxisomal localization of serine: pyruvate aminotransferase in human liver.

T. Noguchi, Y. Takada

Research output: Contribution to journalArticle

38 Citations (Scopus)

Abstract

The distribution of L-serine:pyruvate aminotransferase (EC 2.6.1.51) in human liver was examined by centrifugation in a sucrose density gradient. The enzyme was located only in the peroxisomes and in the soluble fraction. The peroxisomal and soluble enzymes were highly purified and characterized. The two enzyme preparations had nearly identical properties, suggesting that the soluble enzyme is from broken peroxisomes. The two enzyme preparations showed different properties from rat liver serine:pyruvate aminotransferase (Noguchi, T., Okuno, E., and Kido, R. (1976) Biochem. J. 159, 607-613).

Original languageEnglish
Pages (from-to)7598-7600
Number of pages3
JournalJournal of Biological Chemistry
Volume253
Issue number21
Publication statusPublished - Nov 10 1978
Externally publishedYes

Fingerprint

serine-pyruvate aminotransferase
Liver
Enzymes
Peroxisomes
Centrifugation
Sucrose
Rats

ASJC Scopus subject areas

  • Biochemistry

Cite this

Peroxisomal localization of serine : pyruvate aminotransferase in human liver. / Noguchi, T.; Takada, Y.

In: Journal of Biological Chemistry, Vol. 253, No. 21, 10.11.1978, p. 7598-7600.

Research output: Contribution to journalArticle

Noguchi, T. ; Takada, Y. / Peroxisomal localization of serine : pyruvate aminotransferase in human liver. In: Journal of Biological Chemistry. 1978 ; Vol. 253, No. 21. pp. 7598-7600.
@article{b0e187cb0bae40b6bb9ca9d474f85194,
title = "Peroxisomal localization of serine: pyruvate aminotransferase in human liver.",
abstract = "The distribution of L-serine:pyruvate aminotransferase (EC 2.6.1.51) in human liver was examined by centrifugation in a sucrose density gradient. The enzyme was located only in the peroxisomes and in the soluble fraction. The peroxisomal and soluble enzymes were highly purified and characterized. The two enzyme preparations had nearly identical properties, suggesting that the soluble enzyme is from broken peroxisomes. The two enzyme preparations showed different properties from rat liver serine:pyruvate aminotransferase (Noguchi, T., Okuno, E., and Kido, R. (1976) Biochem. J. 159, 607-613).",
author = "T. Noguchi and Y. Takada",
year = "1978",
month = "11",
day = "10",
language = "English",
volume = "253",
pages = "7598--7600",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "21",

}

TY - JOUR

T1 - Peroxisomal localization of serine

T2 - pyruvate aminotransferase in human liver.

AU - Noguchi, T.

AU - Takada, Y.

PY - 1978/11/10

Y1 - 1978/11/10

N2 - The distribution of L-serine:pyruvate aminotransferase (EC 2.6.1.51) in human liver was examined by centrifugation in a sucrose density gradient. The enzyme was located only in the peroxisomes and in the soluble fraction. The peroxisomal and soluble enzymes were highly purified and characterized. The two enzyme preparations had nearly identical properties, suggesting that the soluble enzyme is from broken peroxisomes. The two enzyme preparations showed different properties from rat liver serine:pyruvate aminotransferase (Noguchi, T., Okuno, E., and Kido, R. (1976) Biochem. J. 159, 607-613).

AB - The distribution of L-serine:pyruvate aminotransferase (EC 2.6.1.51) in human liver was examined by centrifugation in a sucrose density gradient. The enzyme was located only in the peroxisomes and in the soluble fraction. The peroxisomal and soluble enzymes were highly purified and characterized. The two enzyme preparations had nearly identical properties, suggesting that the soluble enzyme is from broken peroxisomes. The two enzyme preparations showed different properties from rat liver serine:pyruvate aminotransferase (Noguchi, T., Okuno, E., and Kido, R. (1976) Biochem. J. 159, 607-613).

UR - http://www.scopus.com/inward/record.url?scp=0018265529&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0018265529&partnerID=8YFLogxK

M3 - Article

C2 - 701275

AN - SCOPUS:0018265529

VL - 253

SP - 7598

EP - 7600

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 21

ER -