Table 2.

Mass spectrometric characterization of axonally synthesized proteins

Spot	Protein identification	MS	MS/MS	MW	pI	Accession number
1	Calreticulin	80		48217	4.33	11693172
2	grp78/BiPa	187	122	72667	5.12	109893
3	grp78/BiPa	226	152	72667	5.12	109893
4	β-Actin	125	517	42338	5.29	71620
5	β-Actin	145	476	42338	5.29	71620
6	grp75 precursor	176	129	74272	5.87	2119726
7	HSP70	65		69961	5.44	92355
8	grp75 precursor	73		74272	5.87	2119726
9	β-Actin	85	191	42338	5.29	71620
10	β-Actin	105	155	42338	5.29	71620
11	Vimentin	280		53933	5.06	14389299
12	Vimentin	360	112	53933	5.06	14389299
13	β-Tubulin chain 15	154	226	50665	4.79	92930
14	β-Tubulin chain 15	148	221	50665	4.79	92930
15	β-Tubulin chain 15	87		50665	4.79	92930
16	Peripherin	349	123	53743	5.37	6981416
17	Peripherin	171	76	53743	5.37	6981416
18	HSP60	209	90	58301	5.35	1334284
19	Tropomyosin	43		28854	4.79	7441398
20	γ-Synucleina	58	22	13184	4.68	6755592
26	Dismutase (superoxide dismutase 1)	53	80	15756	5.89	818029
27	ATP synthase subunit d	35		18891	5.78	220904
21	Uch-L1	96		25204	5.12	8394506
22	1-Cys Peroxiredoxin (peroxiredoxin 6)	57		24924	5.64	16758348
23	HSP27	138	134	22952	6.12	1170367
28	α Enolase 1	145	38	47572	6.16	6978809
24	hnRNP H1a	35		49693	5.89	10946928
25	hnRNP H′a	30		49821	5.89	9845253
29	Dimethylarginine dimethylaminohydrolase 2	94	27	25587	5.69	7949035
30	SP22	80		20285	6.32	16924002
31	Erp29	78	35	28694	6.23	16758848
32	Peptidyl isomerase A (cyclophilin A)	100	53	18171	8.34	8394009
33	Cofilin 1, nonmuscle	50	19	18813	8.22	83933101
34	αB crystallin	109	42	19977	6.84	57580
35	Peroxiredoxin 1	110	27	22371	8.27	16923958
36	Glyceraldehyde 3-phosphate dehydrogenase	74	11	36250	8.14	8393418
37	Glyceraldehyde 3-phosphate dehydrogenase	71	11	36250	8.14	8393418
38	Phosphoglycerate kinase 1	88	6	45149	7.53	16757986
39	Phosphoglycerate kinase 1	59		45149	7.53	16757986
40	Aldolase C	123		39654	6.78	1334163

The spot number corresponds to the protein spot numbers indicated in Figure 2. Mass spectra were searched against the National Center for Biotechnology Information database using Mascot software from Matrix Science. For all samples, the tryptic peptide mass fingerprints generated by single-staged mass spectrometry were searched, and the Mascot score is listed under MS. For some of the proteins, tandem mass spectrometry was performed on several peptides, and the Mascot scores of the daughter ion spectra are listed under MS/MS. Protein identities were preferentially selected from the Mascot report based on the species Rattus norvegicus.

^a In several cases in which Mascot scores for R. norvegicus were very low or not listed in the report, the protein identities from Mus musculus were selected. Many distinct proteins were detected as trains of multiple spots, strongly suggesting that the posttranslational modified forms, such as phosphorylation, that alter the pI of the proteins were present.