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A method for the isolation of the amide nitrogen of glutamine from biological samples for mass spectrometry

✍ Scribed by Farook Jahoor; Alan A. Jackson; Michael H.N. Golden

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
511 KB
Volume
121
Category
Article
ISSN
0003-2697

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✦ Synopsis

The amide nitrogen from L-glutamine has been isolated from an artificial plasma, in a form suitable for mass spectrometry, by a macromodification of the glutaminase reaction. The prior removal of free ammonia was carried out by alkaline aeration. When this was performed at 0Β°C for 3 h, spontaneous hydrolysis of glutamine was I .4%. Cross-contamination with nitrogen liberated from the amide group of asparagine can be avoided by preincubation with asparaginase for 2 h and removal of the freed ammonia prior to reacting with glutaminase. Hydrolysis of glutamine during this step is 12%. Measurements of enrichment can be made on samples yielding more than 1 rmol of glutamine amide-derived ammonia.

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