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. 2006 Feb 2;55(10):1247–1257. doi: 10.1007/s00262-005-0108-4

Table 1.

Identification of bovine proTα fragments generated by trypsin1. Fragments T1–T5 were isolated by RP-HPLC (Rt, retention time) and their molecular weight (MW) and primary structure (sequence) were determined by mass spectrometry

Fraction number Rt [min] MW [in Da] ProTα residues Sequence
T1 5.7 849.24 103–109 QKTDEDD
T2 15.0 1564.58 89–102 AAEDDEDDDVDTKK
T3 18.1 1130.44 21–30 EVVEEAENGR
T4 22.9 1466.74 1–14 SDAAVDTSSEITTK
T5 26.9 6144.07 31–87 EAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGK

1 Bovine proTα: acSDAAVDTSSEITTKDLKEKKEVVEEAENGR ↓ EAPANGNANEENGEQEADNEVDEEEE

Human proTα: acSDAAVDTSSEITTK DLKEKK EVVEEAENGR DAPANGNANEENGEQEADNEVDEEEE

EGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD

EGGEEEEEEEEGDGEEEDGDEDEEAE S ATGK R AAEDDEDDDVDTKK QKTDEDD

Primary structures of bovine and human proTα are overlayed. Arrows (↓) indicate where tryptic cleavages occurred

Bold letters indicate differences in the amino acid sequences of the two polypeptides