In vitro covalent modification of serum albumin by acrolein

Jose C. Gan, Aileen Oandasan, Ghulam Ansari

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Amino acid analyses of human serum albumin treated with acrolein under in vitro conditions showed disappearance of lysine and histidine residues with concomitant appearance of four new peaks upon amino acid analyses. The first three peaks emerged just prior to histidine, while the fourth emerged between ammonia and arginine. Model compound (polyhistidine) treated with acrolein and subjected to amino acid analyses provided three peaks which eluted at the same positions as the first three peaks found in the acrolein-treated albumin. This provided tentative identification of the first three peaks as possible histindine-acrolein adducts. Likewise, model compound polylysine treated under the same conditions yielded a peak which corresponded to the fourth peak observed in the acrolein-treated albumin. There is a direct proportional increase in the adducts formed with increasing concentrations of acrolein. The chemical caused substantial increase in the absorbance of albumin at 280 nm indicating unfolding of the protein. Covalent modifications of the lysine and histidine residues by acrolein do not have any effect on the binding of palmitic acid or bromcresol green to albumin.

Original languageEnglish (US)
Pages (from-to)939-947
Number of pages9
JournalChemosphere
Volume23
Issue number7
DOIs
StatePublished - 1991

Fingerprint

Acrolein
Serum Albumin
Amino acids
serum
amino acid
Albumins
Palmitic acid
Histidine
Arginine
absorbance
Ammonia
Amino Acids
Lysine
ammonia
Bromcresol Green
Proteins
protein
acid
Protein Unfolding
Polylysine

ASJC Scopus subject areas

  • Environmental Science(all)
  • Environmental Chemistry

Cite this

In vitro covalent modification of serum albumin by acrolein. / Gan, Jose C.; Oandasan, Aileen; Ansari, Ghulam.

In: Chemosphere, Vol. 23, No. 7, 1991, p. 939-947.

Research output: Contribution to journalArticle

Gan, Jose C. ; Oandasan, Aileen ; Ansari, Ghulam. / In vitro covalent modification of serum albumin by acrolein. In: Chemosphere. 1991 ; Vol. 23, No. 7. pp. 939-947.
@article{c234ec5b9c224f629cc4107ad1ccfef5,
title = "In vitro covalent modification of serum albumin by acrolein",
abstract = "Amino acid analyses of human serum albumin treated with acrolein under in vitro conditions showed disappearance of lysine and histidine residues with concomitant appearance of four new peaks upon amino acid analyses. The first three peaks emerged just prior to histidine, while the fourth emerged between ammonia and arginine. Model compound (polyhistidine) treated with acrolein and subjected to amino acid analyses provided three peaks which eluted at the same positions as the first three peaks found in the acrolein-treated albumin. This provided tentative identification of the first three peaks as possible histindine-acrolein adducts. Likewise, model compound polylysine treated under the same conditions yielded a peak which corresponded to the fourth peak observed in the acrolein-treated albumin. There is a direct proportional increase in the adducts formed with increasing concentrations of acrolein. The chemical caused substantial increase in the absorbance of albumin at 280 nm indicating unfolding of the protein. Covalent modifications of the lysine and histidine residues by acrolein do not have any effect on the binding of palmitic acid or bromcresol green to albumin.",
author = "Gan, {Jose C.} and Aileen Oandasan and Ghulam Ansari",
year = "1991",
doi = "10.1016/0045-6535(91)90098-X",
language = "English (US)",
volume = "23",
pages = "939--947",
journal = "Chemosphere",
issn = "0045-6535",
publisher = "Elsevier Limited",
number = "7",

}

TY - JOUR

T1 - In vitro covalent modification of serum albumin by acrolein

AU - Gan, Jose C.

AU - Oandasan, Aileen

AU - Ansari, Ghulam

PY - 1991

Y1 - 1991

N2 - Amino acid analyses of human serum albumin treated with acrolein under in vitro conditions showed disappearance of lysine and histidine residues with concomitant appearance of four new peaks upon amino acid analyses. The first three peaks emerged just prior to histidine, while the fourth emerged between ammonia and arginine. Model compound (polyhistidine) treated with acrolein and subjected to amino acid analyses provided three peaks which eluted at the same positions as the first three peaks found in the acrolein-treated albumin. This provided tentative identification of the first three peaks as possible histindine-acrolein adducts. Likewise, model compound polylysine treated under the same conditions yielded a peak which corresponded to the fourth peak observed in the acrolein-treated albumin. There is a direct proportional increase in the adducts formed with increasing concentrations of acrolein. The chemical caused substantial increase in the absorbance of albumin at 280 nm indicating unfolding of the protein. Covalent modifications of the lysine and histidine residues by acrolein do not have any effect on the binding of palmitic acid or bromcresol green to albumin.

AB - Amino acid analyses of human serum albumin treated with acrolein under in vitro conditions showed disappearance of lysine and histidine residues with concomitant appearance of four new peaks upon amino acid analyses. The first three peaks emerged just prior to histidine, while the fourth emerged between ammonia and arginine. Model compound (polyhistidine) treated with acrolein and subjected to amino acid analyses provided three peaks which eluted at the same positions as the first three peaks found in the acrolein-treated albumin. This provided tentative identification of the first three peaks as possible histindine-acrolein adducts. Likewise, model compound polylysine treated under the same conditions yielded a peak which corresponded to the fourth peak observed in the acrolein-treated albumin. There is a direct proportional increase in the adducts formed with increasing concentrations of acrolein. The chemical caused substantial increase in the absorbance of albumin at 280 nm indicating unfolding of the protein. Covalent modifications of the lysine and histidine residues by acrolein do not have any effect on the binding of palmitic acid or bromcresol green to albumin.

UR - http://www.scopus.com/inward/record.url?scp=0025936368&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0025936368&partnerID=8YFLogxK

U2 - 10.1016/0045-6535(91)90098-X

DO - 10.1016/0045-6535(91)90098-X

M3 - Article

VL - 23

SP - 939

EP - 947

JO - Chemosphere

JF - Chemosphere

SN - 0045-6535

IS - 7

ER -