• P-ISSN2233-4203
  • E-ISSN2093-8950

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  • P-ISSN 2233-4203
  • E-ISSN 2093-8950

Effects of Temperature and Acetonitrile on Microwave-Assisted Weak Acid Protein Hydrolysis

Mass Spectrometry Letters, (P)2233-4203; (E)2093-8950
2018, v.9 no.2, pp.46-50
https://doi.org/10.5478/MSL.2018.9.2.46
Nam Mihyeon (Chungnam National University)
Lee Dabin (Chungnam National University)
Kim Yeoseon (Chungnam National University)
Kim Jeongkwon (Chungnam National University)
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Abstract

The effects of temperature and acetonitrile (ACN) concentration on microwave-assisted weak-acid hydrolysis of pro- teins were investigated. Myoglobin was hydrolyzed for 1 h using 2% formic acid and a microwave with different concentrations of ACN (0, 5, and 10%) at various temperatures (50, 60, 70, 80, 90, and 100 o C). The numbers of peptides identified with each concentration of ACN were the same for each temperature. The greatest number of peptides (18 total) was obtained with hydro- lysis at 100 o C, and 6 of these were a result of additional removal of aspartic acid at the C-terminus. Hydrolysis at 80 o C resulted in 13 peptides, of which only 1 was generated by the additional removal of aspartic acid, and 12 were observed with hydrolysis at 100 o C. Our results demonstrate that microwave-assisted weak-acid hydrolysis of proteins can be performed successfully at 80 o C, which could be beneficial for limiting side reactions and generating larger peptide sequences.

keywords
Microwave MALDI Acid hydrolysis Acetonitrile Temperature


Reference

1

Miyeong Seo. (2012). Microwave-assisted Weak Acid Hydrolysis of Proteins. Mass Spectrometry Letters, 3(2), 47-49. http://dx.doi.org/10.5478/MSL.2012.3.2.47.

2

서미영. (2013). Weak Acid Hydrolysis of Proteins. Bulletin of the Korean Chemical Society, 34(1), 27-28. http://dx.doi.org/10.5012/bkcs.2013.34.1.27.

3

Cannon, J.. (2010). . J. Proteome Res., 9, 3886-. http://dx.doi.org/10.1021/pr1000994.

4

Remily-Wood, E.. (2009). . J. Am. Soc. Mass Spectrom., 20, 2106-. http://dx.doi.org/10.1016/j.jasms.2009.07.007.

5

Tsiatsiani, L.. (2015). . FEBS J., 282, 2612-. http://dx.doi.org/10.1111/febs.13287.

6

Swatkoski, S.. (2007). . J. Proteome Res., 6, 4525-. http://dx.doi.org/10.1021/pr0704682.

7

Yang, H. -J.. (2010). . Rapid Commun. Mass Spectrom., 24, 901-. http://dx.doi.org/10.1002/rcm.4467.

8

Chen, W. Y.. (2007). . Anal. Chem., 79, 2394-. http://dx.doi.org/10.1021/ac0614893.

9

Russell, W. K.. (2001). . Anal. Chem., 73, 2682-. http://dx.doi.org/10.1021/ac001332p.

10

Park, S.. (2013). . Rapid Commun. Mass Spectrom., 27, 842-. http://dx.doi.org/10.1002/rcm.6508.

11

Wu, C.. (2012). . Nat. Methods, 9, 822-. http://dx.doi.org/10.1038/nmeth.2074.

12

Koomen, J. M.. (2005). . J. Proteome Res., 4, 972-. http://dx.doi.org/10.1021/pr050046x.

Submission Date
2018-02-21
Revised Date
2018-03-03
Accepted Date
2018-03-12
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