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Assessing the multimeric states of proteins: Studies using laser desorption mass spectrometry

✍ Scribed by Terry B. Farmer; Richard M. Caprioli

Publisher: John Wiley and Sons
Year: 1991
Tongue: English
Weight: 419 KB
Volume: 20
Category: Article
ISSN: 1076-5174
DOI: 10.1002/bms.1200201209

No coin nor oath required. For personal study only.

✦ Synopsis

We have developed a technique which utilizes matrix-assisted laser desorption mass spectrometry to study the subunit association of proteins. Aqueous protein samples are treated with a dilute solution of glutaraldehyde, a cross-linking agent which reacts with free amino groups on proteins. This agent effectively traps the multimeric form, preventing it from dissociating in the sample preparation and desorption process. Proteins measured include lysozyme, carbonic anhydrase, apomyoglobin, glucose 6-phosphate dehydrogenase, ovine lutropin, yeast alcohol dehydrogenase, avidin and pyruvate kinase. Dimeric and tetrameric complexes up to 250,000 Da have been measured in this manner.

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