Mini-chromatofocusing of plant and fungal polyphenoloxidases

Bob Moore, William H. Flurkey

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Mini-chromatofocusing was used to estimate the isoelectric points of mung bean polyphenoloxidase (5.4), broad bean polyphenoloxidase (5.4-5.7), and mushroom tyrosinase (4.5) in crude and purified samples. Using 1 to 2 ml of Polybuffer exchanger and 20 to 25 ml of Polybuffer 74, isoelectric points for the above enzymes were obtained in less than 2 h. Using this technique, isoelectric points for β-lactoglobulin (4.5), carbonic anhydrase (6.4), soybean trypsin inhibitor (4.1), myoglobin (6.9), and bovine serum albumin (4.8) were obtained and compared to existing literature values. Mini-chromatofocusing provides a rapid estimation for isoelectric points of proteins and enzymes and may be a useful alternative to conventional methods for determination of isoelectric points.

Original languageEnglish (US)
Pages (from-to)504-508
Number of pages5
JournalAnalytical Biochemistry
Volume172
Issue number2
DOIs
StatePublished - Aug 1 1988
Externally publishedYes

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Catechol Oxidase
Isoelectric Point
Lactoglobulins
Carbonic Anhydrases
Trypsin Inhibitors
Monophenol Monooxygenase
Myoglobin
Enzymes
Bovine Serum Albumin
Agaricales
Proteins
Soybeans

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Mini-chromatofocusing of plant and fungal polyphenoloxidases. / Moore, Bob; Flurkey, William H.

In: Analytical Biochemistry, Vol. 172, No. 2, 01.08.1988, p. 504-508.

Research output: Contribution to journalArticle

Moore, Bob ; Flurkey, William H. / Mini-chromatofocusing of plant and fungal polyphenoloxidases. In: Analytical Biochemistry. 1988 ; Vol. 172, No. 2. pp. 504-508.
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