Letter: Correlation between phosphorylation ratios by matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis and enzyme kinetics

Jeong Hun Kang; Masanori Kuramoto; Akira Tsuchiya; Riki Toita; Daisuke Asai; Yuko T. Sato; Takeshi Mori; Takuro Niidome; Yoshiki Katayama

doi:10.1255/ejms.916

Letter: Correlation between phosphorylation ratios by matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis and enzyme kinetics

Jeong Hun Kang, Masanori Kuramoto, Akira Tsuchiya, Riki Toita, Daisuke Asai, Yuko T. Sato, Takeshi Mori, Takuro Niidome, Yoshiki Katayama

Oral Rehabilitation

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Abstract

To identify the correlation between the phosphorylation ratios by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-ToF MS) analysis and enzyme kinetics (K_m, V_max and V_max/K_m) it is important to understand whether MALDI-ToF MS can be applied for monitoring the properties of peptides that are substrates of protein kinases. The correlation between phosphorylation ratios and enzyme kinetics was examined using peptides for protein kinase C (PKC) and for 60 kDa phosphoprotein, encoded by the cellular sarcoma gene (c-Src). Phosphorylation ratios, analyzed by MALDI-ToF MS, showed a higher correlation coefficient (r=>+0.7) for V_max/K_m compared with that (r= < ±0.6) for K_m or V_max. For ion modes, a higher correlation coefficient between phosphorylation ratios and V_max/ K_m was identified in the positive mode (r=> + 0.7) compared with that in the negative mode (r=<+0.5). These results suggest that MALDI-ToF MS is a useful tool to evaluate V_max/K_max of peptides for protein kinases.

Original language	English
Pages (from-to)	261-265
Number of pages	5
Journal	European Journal of Mass Spectrometry
Volume	14
Issue number	4
DOIs	https://doi.org/10.1255/ejms.916
Publication status	Published - 2008

All Science Journal Classification (ASJC) codes

Atomic and Molecular Physics, and Optics
Spectroscopy

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Kang, J. H., Kuramoto, M., Tsuchiya, A., Toita, R., Asai, D., Sato, Y. T., Mori, T., Niidome, T., & Katayama, Y. (2008). Letter: Correlation between phosphorylation ratios by matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis and enzyme kinetics. European Journal of Mass Spectrometry, 14(4), 261-265. https://doi.org/10.1255/ejms.916

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title = "Letter: Correlation between phosphorylation ratios by matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis and enzyme kinetics",

abstract = "To identify the correlation between the phosphorylation ratios by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-ToF MS) analysis and enzyme kinetics (Km, Vmax and Vmax/Km) it is important to understand whether MALDI-ToF MS can be applied for monitoring the properties of peptides that are substrates of protein kinases. The correlation between phosphorylation ratios and enzyme kinetics was examined using peptides for protein kinase C (PKC) and for 60 kDa phosphoprotein, encoded by the cellular sarcoma gene (c-Src). Phosphorylation ratios, analyzed by MALDI-ToF MS, showed a higher correlation coefficient (r=>+0.7) for Vmax/Km compared with that (r= < ±0.6) for Km or Vmax. For ion modes, a higher correlation coefficient between phosphorylation ratios and Vmax/ Km was identified in the positive mode (r=> + 0.7) compared with that in the negative mode (r=<+0.5). These results suggest that MALDI-ToF MS is a useful tool to evaluate Vmax/Kmax of peptides for protein kinases.",

author = "Kang, {Jeong Hun} and Masanori Kuramoto and Akira Tsuchiya and Riki Toita and Daisuke Asai and Sato, {Yuko T.} and Takeshi Mori and Takuro Niidome and Yoshiki Katayama",

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AU - Kang, Jeong Hun

AU - Kuramoto, Masanori

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AU - Toita, Riki

AU - Asai, Daisuke

AU - Sato, Yuko T.

AU - Mori, Takeshi

AU - Niidome, Takuro

AU - Katayama, Yoshiki

PY - 2008

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AB - To identify the correlation between the phosphorylation ratios by matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-ToF MS) analysis and enzyme kinetics (Km, Vmax and Vmax/Km) it is important to understand whether MALDI-ToF MS can be applied for monitoring the properties of peptides that are substrates of protein kinases. The correlation between phosphorylation ratios and enzyme kinetics was examined using peptides for protein kinase C (PKC) and for 60 kDa phosphoprotein, encoded by the cellular sarcoma gene (c-Src). Phosphorylation ratios, analyzed by MALDI-ToF MS, showed a higher correlation coefficient (r=>+0.7) for Vmax/Km compared with that (r= < ±0.6) for Km or Vmax. For ion modes, a higher correlation coefficient between phosphorylation ratios and Vmax/ Km was identified in the positive mode (r=> + 0.7) compared with that in the negative mode (r=<+0.5). These results suggest that MALDI-ToF MS is a useful tool to evaluate Vmax/Kmax of peptides for protein kinases.

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Letter: Correlation between phosphorylation ratios by matrix-assisted laser desorption/ionization time-of-flight mass spectrometric analysis and enzyme kinetics

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