Table 3.

Correspondence between peptide fragments of bovine dihydrolipoamide dehydrogenase and the mol. masses of the peptides after tryptic digestion of the mitochondrial protein catalyzing NADH-supported, ammonium-stimulated H₂O₂ production as determined by MALDI analysis^a

Amino acid residue numbersb	Mr of matched peptidesc		Peptide assigned
	Observed	Calculated
60–66	734.3933	733.4123	K.AAQLGFK.T
90–104	1721.9225	1720.8797	K.ALLNNSHFYHLAHGK.D
90–109	2298.1630	2297.1454	K.ALLNNSHFYHLAHGKDFASR.G
110–117	920.4668	919.4433	R.GIEMSEVR.L
110–117	936.4639	935.4382	R.GIEMSEVR.L Oxidation (M)
110–122	1533.8313	1532.7868	R.GIEMSEVRLNLEK.M Oxidation (M)
133–143	1127.6952	1126.6499	K.ALTGGIAHLFK.Q
316–334	2201.1873	2200.1488	R.RPFTQNLGLEELGIELDTR.G
347–365	1995.1301	1994.0659	K.IPNIYAIGDVVAGPMLAHK.A Oxidation (M)
405–417	1581.8074	1580.7569	K.SEEQLKEEGIEYK.V
418–428	1193.6822	1192.6353	K.VGKFPFAANSR.A
421–428	909.4682	908.4504	K.FPFAANSR.A
483–495	1467.7734	1466.7089	R.VCHAHPTLSEAFR.E
483–495	1538.7980	1537.7460	R.VCHAHPTLSEAFR.E Propionamide (C)
496–505	1007.5454	1006.5083	R.EANLAASFGK.S

^aProtein score of 142 for bovine dihydrolipoamide dehydrogenase (accession in NCBI database gil76615127) with cut-off value of 82 for p<0.05 confidence. Sequence coverage was 26%. No search for specific posttranslation modifications was done.

^bIn bovine dihydrolipoamide dehydrogenase.

^cFor peptides after tryptic digestion of the band shown in Fig. 1 B. Seven peptides not matched to dihydrolipoamide dehydrogenase sequence were present in small amount thus suggesting slight contamination of the band by other protein(s).