Table III.
Molecular analysis of the purified AMP fractions
| Protein Fraction | Molecular Mass Determined by:
|
Amino Acid Sequence
|
|||
|---|---|---|---|---|---|
| Matrix-assisted laser-desorption ionization time of flight MS | Electrospray ionization-MS | Theoretical prediction | Determined amino terminal | Predicted carboxy terminal | |
| D | |||||
| p3105EF1 | 5,614 ± 5 | 5,608.3 ± 1 | 5,604.25 | ELCEKAS | CYFNCS |
| p3105EF2 | 5,602 ± 5 | 5,604.9 ± 1 | 5,604.25 | ELCEKAS | CYFNCS |
| p3105EF3 | 6,223 ± 6 | nda | 6,225.15 | DVEPGQK | ICYFPC |
Molecular mass (D) of DmAMP1-CRPs and RsAFP2-CRPs purified as described in Fig. 3 was determined by matrix-assisted laser-desorption-ionization time of flight or electrospray ionization-mass spectrometry (MS) and amino-terminal sequence of the same components was determined by automated Edman degradation. Also shown are the predicted carboxy-terminal sequences that give best correspondence between experimental molecular mass and theoretical molecular mass. Amino acids of the mature DmAMP1 domain are underlined, amino acids of the linker peptide are in bold, and amino acids of the mature RsAFP2 domain are italicized.
a
nd, Not determined.