Purification and characterization of a blue-colored red-fluorescent protein from the silkworm (Bombyx mori L.) larvae

Michio Doi, Yuzo Shioi, Tsutomu Sasa

Research output: Contribution to journalArticle

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Abstract

1. 1. A red-fluorescent blue protein (P600) was purified from the digestive juice of the silkworm (Bombyx mori L.) larvae raised on mulberry leaves. 2. 2. The purified protein was electrophoretically homogeneous and showed the absorption maxima at 601.5 nm and 278 nm, and the fluorescence maximum at 621 nm. 3. 3. The molecular weight was estimated to be 540,000 by gel filtration on Sepharose CL-6B. Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate suggests that the protein consists of two heterogeneous polypeptide subunits with a mol. wt of 15,000 and 18,000. 4. 4. The P600 contains excess acidic amino acid residues over basic groups. The polarity and pI were 45.5% and 4.6, respectively. 5. 5. The production of H2O2 was observed in the presence of P600 upon illumination.

Original languageEnglish
Pages (from-to)569-573
Number of pages5
JournalComparative Biochemistry and Physiology -- Part B: Biochemistry and
Volume83
Issue number3
DOIs
Publication statusPublished - Jan 1 1986

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Bombyx
Purification
Larva
Acidic Amino Acids
Morus
Lighting
Sodium Dodecyl Sulfate
Gel Chromatography
Polyacrylamide Gel Electrophoresis
Proteins
Molecular Weight
Fluorescence
Electrophoresis
Peptides
Gels
Molecular weight
red fluorescent protein
sepharose CL 6B

All Science Journal Classification (ASJC) codes

  • Physiology
  • Biochemistry
  • Molecular Biology

Cite this

Purification and characterization of a blue-colored red-fluorescent protein from the silkworm (Bombyx mori L.) larvae. / Doi, Michio; Shioi, Yuzo; Sasa, Tsutomu.

In: Comparative Biochemistry and Physiology -- Part B: Biochemistry and, Vol. 83, No. 3, 01.01.1986, p. 569-573.

Research output: Contribution to journalArticle

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