Abnormal tau proteins from alzheimer's disease brains purification and amino acid analysis

Wan Kyng Liu, Hanna Ksiezak-Reding, Shu Hui Yen

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Abnormal tau proteins (PHF-tau) were isolated from Alzheimer's disease brains by treatment of paired helical filament enriched-fractions with perchloric acid and boiling of the acid precipitable fraction with β-mercaptoethanol. These proteins were purified further by a second perchloric acid treatment. The purified PHF-tau proteins were soluble in buffers devoid of sodium dodecyl sulfate. However, they were similar to the abnormal tau extracted from paired helical filaments with sodium dodecyl sulfate, also named A68, in molecular mass (68, 64, and 60 kDa), isoelectric point (pI 5.5-6.5), reactivity with anti-tau antibodies, and in requirement for alkaline phosphatase treatment to bind the Tau-1 antibody. Compared to normal tau, the soluble PHF-tau contained 100% more glycine and 35% less lysine residue. The results suggest that besides phosphorylation other types of modification may be involved in differentiating PHF-tau from normal tau.

Original languageEnglish (US)
Pages (from-to)21723-21727
Number of pages5
JournalJournal of Biological Chemistry
Volume266
Issue number32
StatePublished - 1991
Externally publishedYes

Fingerprint

tau Proteins
Sodium Dodecyl Sulfate
Purification
Brain
Alzheimer Disease
Amino Acids
Phosphorylation
Mercaptoethanol
Antibodies
Isoelectric Point
Molecular mass
Glycine
Boiling liquids
Lysine
Alkaline Phosphatase
Anti-Idiotypic Antibodies
Buffers
Acids
Proteins
Perchloric Acid

ASJC Scopus subject areas

  • Biochemistry

Cite this

Abnormal tau proteins from alzheimer's disease brains purification and amino acid analysis. / Liu, Wan Kyng; Ksiezak-Reding, Hanna; Yen, Shu Hui.

In: Journal of Biological Chemistry, Vol. 266, No. 32, 1991, p. 21723-21727.

Research output: Contribution to journalArticle

Liu, WK, Ksiezak-Reding, H & Yen, SH 1991, 'Abnormal tau proteins from alzheimer's disease brains purification and amino acid analysis', Journal of Biological Chemistry, vol. 266, no. 32, pp. 21723-21727.
Liu, Wan Kyng ; Ksiezak-Reding, Hanna ; Yen, Shu Hui. / Abnormal tau proteins from alzheimer's disease brains purification and amino acid analysis. In: Journal of Biological Chemistry. 1991 ; Vol. 266, No. 32. pp. 21723-21727.
@article{94463a0c1903485f9fb59b5e3bec8992,
title = "Abnormal tau proteins from alzheimer's disease brains purification and amino acid analysis",
abstract = "Abnormal tau proteins (PHF-tau) were isolated from Alzheimer's disease brains by treatment of paired helical filament enriched-fractions with perchloric acid and boiling of the acid precipitable fraction with β-mercaptoethanol. These proteins were purified further by a second perchloric acid treatment. The purified PHF-tau proteins were soluble in buffers devoid of sodium dodecyl sulfate. However, they were similar to the abnormal tau extracted from paired helical filaments with sodium dodecyl sulfate, also named A68, in molecular mass (68, 64, and 60 kDa), isoelectric point (pI 5.5-6.5), reactivity with anti-tau antibodies, and in requirement for alkaline phosphatase treatment to bind the Tau-1 antibody. Compared to normal tau, the soluble PHF-tau contained 100{\%} more glycine and 35{\%} less lysine residue. The results suggest that besides phosphorylation other types of modification may be involved in differentiating PHF-tau from normal tau.",
author = "Liu, {Wan Kyng} and Hanna Ksiezak-Reding and Yen, {Shu Hui}",
year = "1991",
language = "English (US)",
volume = "266",
pages = "21723--21727",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "32",

}

TY - JOUR

T1 - Abnormal tau proteins from alzheimer's disease brains purification and amino acid analysis

AU - Liu, Wan Kyng

AU - Ksiezak-Reding, Hanna

AU - Yen, Shu Hui

PY - 1991

Y1 - 1991

N2 - Abnormal tau proteins (PHF-tau) were isolated from Alzheimer's disease brains by treatment of paired helical filament enriched-fractions with perchloric acid and boiling of the acid precipitable fraction with β-mercaptoethanol. These proteins were purified further by a second perchloric acid treatment. The purified PHF-tau proteins were soluble in buffers devoid of sodium dodecyl sulfate. However, they were similar to the abnormal tau extracted from paired helical filaments with sodium dodecyl sulfate, also named A68, in molecular mass (68, 64, and 60 kDa), isoelectric point (pI 5.5-6.5), reactivity with anti-tau antibodies, and in requirement for alkaline phosphatase treatment to bind the Tau-1 antibody. Compared to normal tau, the soluble PHF-tau contained 100% more glycine and 35% less lysine residue. The results suggest that besides phosphorylation other types of modification may be involved in differentiating PHF-tau from normal tau.

AB - Abnormal tau proteins (PHF-tau) were isolated from Alzheimer's disease brains by treatment of paired helical filament enriched-fractions with perchloric acid and boiling of the acid precipitable fraction with β-mercaptoethanol. These proteins were purified further by a second perchloric acid treatment. The purified PHF-tau proteins were soluble in buffers devoid of sodium dodecyl sulfate. However, they were similar to the abnormal tau extracted from paired helical filaments with sodium dodecyl sulfate, also named A68, in molecular mass (68, 64, and 60 kDa), isoelectric point (pI 5.5-6.5), reactivity with anti-tau antibodies, and in requirement for alkaline phosphatase treatment to bind the Tau-1 antibody. Compared to normal tau, the soluble PHF-tau contained 100% more glycine and 35% less lysine residue. The results suggest that besides phosphorylation other types of modification may be involved in differentiating PHF-tau from normal tau.

UR - http://www.scopus.com/inward/record.url?scp=0025719441&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025719441&partnerID=8YFLogxK

M3 - Article

C2 - 1939196

AN - SCOPUS:0025719441

VL - 266

SP - 21723

EP - 21727

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 32

ER -