Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry.

Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Research Abstract Details 

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Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Abstract Text:

Chunling Wa,Ron L Cerny,David S Hage,

A method was developed for characterizing immobilization sites on a protein based on stable isotope labeling and MALDI-TOF mass spectrometry. The model for this work was human serum albumin (HSA) immobilized onto silica by the Schiff base method. The immobilized HSA was digested by various proteolytic enzymes in the presence of normal water, while soluble HSA was digested in (18)O-enriched water for use as an internal standard. These two digests were mixed and analyzed, with the (18)O/(16)O ratio for each detected peptide then being measured. Several peptides in the tryptic, Lys-C, and Glu-C digests gave significantly higher (18)O/(16)O ratios than other peptides in the same digests, implying their involvement in immobilization. Analysis of these results led to identification of the N-terminus and several lysines as likely immobilization sites for HSA (e.g., K4, K41, K190, K225, K313, and K317). It was also possible from these results to quantitatively rank these sites in terms of the relative degree to which each might take part in immobilization. This method is not limited to HSA and silica but can be used with other proteins and supports.

Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Publishing Authors By Initials

C Wa,RL Cerny,DS Hage,

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PUBMED ID PMID:

MEDLINE DATE:

Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Analytical chemistry

VOLUME: 78

Page Numbers: 7967-77

Journal Abbreviation: Anal. Chem.

ISSN: 0003-2700

DAY: 1

MONTH: Dec

YEAR: 2006

Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370536

Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Keywords Mesh Terms:

KEYWORDS: Spectrometry, Mass, Matrix-Assisted Lase

MESH TERMS: methods

Chemical & Substance for Abstract: Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry. Information

Substance Name: Lysine

Registry Number: 56-87-1

Grant and Affiliation Information for Identification and quantitative studies of protein immobilization sites by stable isotope labeling and mass spectrometry.

AFFILIATION: Department of Chemistry, University of Nebraska-Lincoln, Lincoln, NE 68588-0304, USA.

Country: United States

AGENCY: United States NCRR

GRANT: RR 015468-01

ACRONYM: RR

MEDLINETA: Anal Chem

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