Equine myoglobin

Figure 2.9. Schematic of a matrix-assisted laser desorption/ionization (MALDI) event. The SEM micrograph depicts sinapinic acid-equine myoglobin crystal from a sample prepared according to the dried drop sample preparation method. In the desorption event neutral matrix molecules (M), positive matrix ions (M+), negative matrix ions (M-), neutral analyte molecules (N), positive analyte ions (+), and negative analyte ions (-) are created and/or transferred to the gas phase. Reprinted from A. Westman-Brinkmalm and G. Brinkmalm (2002). In Mass Spectrometry and Hyphenated Techniques in Neuropeptide Research, J. Silberring and R. Ekman (eds.) New York John Wiley Sons, 47-105. With permission of John Wiley Sons, Inc.

Figure 9.9 ESI mass spectra of two proteins (a) hen egg-white lysozyme and (b) equine myoglobin.

FIGURE 8.4 Normalized cross-sections vs corrected arrival times for myoglobin. Plot used to create a cross-section calibration for the Synapt instrument. The sample analyzed was equine myoglobin and charge states [M-h8H] +-[M-h 16H] + were used. 

A related approach at a molecular level has been used, with methyl- Cs-MNP to examine the proximity of the spin-adduct methyl groups to aromatic tyrosine and phenylalanine protons in equine myoglobin. By use of this approach it has been shown that radical generation and hence spin-adduct formation occurs solely at the Tyr-103 residue. ... 

Figure 18.8. High-resolution nanoESI mass spectrum of equine myoglobin (0.2 mg mL pH 7.5, lOmM NH4HCO3) with a 7-tesla FT-ICR mass spectrometer (lonSpec Ultima).

Enzymatic microreactors (7.5 nL) have been fabricated in the microfluidic chip to prepare the tryptic digest of equine (horse) myoglobin (14.2 pmol/p.L)... 

Amyloglucosidase (Aspergillus niger) 3.6 Myoglobin (equine heart) 7.2... 

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