Identification of retinol as one of the protein HC chromophores
Escribano, Julio ; Grubb, Anders LU
and Méndez, Enrique
(1988)
In Biochemical and Biophysical Research Communications
155(3).
p.1424-1429
- Abstract
Protein HC (alias alpha 1-microglobulin) contains so far unidentified yellow-brown fluorescent chromophores. Several preparations of human protein HC were extracted with hexane. Most of the extracts contained a substance which, upon reversed-phase HPLC, co-eluted with all-trans- retinol and had an absorption spectrum identical to that of retinol. The substance was also, like retinol, destroyed by exposure to ultraviolet light and acid pH. These observations strongly support the proposal that protein HC is a member of the newly defined lipocalin protein superfamily. The highest retinol-protein HC molar ratio of the investigated protein HC preparations was 1.6 x 10(-3) indicating that retinol is not the only ligand bound to protein HC.... (More)
Protein HC (alias alpha 1-microglobulin) contains so far unidentified yellow-brown fluorescent chromophores. Several preparations of human protein HC were extracted with hexane. Most of the extracts contained a substance which, upon reversed-phase HPLC, co-eluted with all-trans- retinol and had an absorption spectrum identical to that of retinol. The substance was also, like retinol, destroyed by exposure to ultraviolet light and acid pH. These observations strongly support the proposal that protein HC is a member of the newly defined lipocalin protein superfamily. The highest retinol-protein HC molar ratio of the investigated protein HC preparations was 1.6 x 10(-3) indicating that retinol is not the only ligand bound to protein HC. This was confirmed by comparing the absorption spectrum of protein HC before and after hexane extraction.
(Less)
- author
- Escribano, Julio
; Grubb, Anders
LU
and Méndez, Enrique
- organization
- publishing date
- 1988
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Alpha-Globulins/metabolism, Chromatography, High Pressure Liquid, Humans, Vitamin A/metabolism
- in
- Biochemical and Biophysical Research Communications
- volume
- 155
- issue
- 3
- pages
- 1424 - 1429
- publisher
- Elsevier
- external identifiers
-
- pmid:2460097
- scopus:0023813270
- ISSN
- 0006-291X
- DOI
- 10.1016/s0006-291x(88)81300-7
- language
- English
- LU publication?
- yes
- id
- fac16765-659d-4702-a334-00f3c0a64bd1
- date added to LUP
- 2021-10-27 08:07:03
- date last changed
- 2024-01-12 02:55:38
@article{fac16765-659d-4702-a334-00f3c0a64bd1,
abstract = {{<p>Protein HC (alias alpha 1-microglobulin) contains so far unidentified yellow-brown fluorescent chromophores. Several preparations of human protein HC were extracted with hexane. Most of the extracts contained a substance which, upon reversed-phase HPLC, co-eluted with all-trans- retinol and had an absorption spectrum identical to that of retinol. The substance was also, like retinol, destroyed by exposure to ultraviolet light and acid pH. These observations strongly support the proposal that protein HC is a member of the newly defined lipocalin protein superfamily. The highest retinol-protein HC molar ratio of the investigated protein HC preparations was 1.6 x 10(-3) indicating that retinol is not the only ligand bound to protein HC. This was confirmed by comparing the absorption spectrum of protein HC before and after hexane extraction.</p>}},
author = {{Escribano, Julio and Grubb, Anders and Méndez, Enrique}},
issn = {{0006-291X}},
keywords = {{Alpha-Globulins/metabolism; Chromatography, High Pressure Liquid; Humans; Vitamin A/metabolism}},
language = {{eng}},
number = {{3}},
pages = {{1424--1429}},
publisher = {{Elsevier}},
series = {{Biochemical and Biophysical Research Communications}},
title = {{Identification of retinol as one of the protein HC chromophores}},
url = {{http://dx.doi.org/10.1016/s0006-291x(88)81300-7}},
doi = {{10.1016/s0006-291x(88)81300-7}},
volume = {{155}},
year = {{1988}},
}