[原著］Exposure of threony 1 residue at position 10 in fibrinopeptide A is essential to the recognition by habutobin
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We have reported that habutobin acted only on rabbit fibrinogen by cleaving the Arg^16-Gly^17 bond in the A$ \alpha $ chain. We have also demonstrated that habutobin recognized threonine (Thr) at position 10 from the COOH-end of the rabbit fibrinopeptide A (FPA). Since Thr has been revealed to also exist at position 10 in chicken FPA, we postulated that habutobin may recognize chicken Thr, thereby converting it into fibrin gel. We investigated whether habutobin acted on chicken fibrinogen to form fibrin gel. Habutobin clotted chicken fibrinogen more slowly than it did rabbit fibrinogen. It clotted the chicken fibrinogen with a resultant release of three peptides (peak I, II and X peptides), whereas thrombin clotted the chicken fibrinogen with a resultant release of two peptides (peak 1 and 2 peptides). The elution times of the peak I and II peptides were identical to those of peak 1 and 2 peptides. The peak 2 fibrmopeptide was identified as the FPA of chicken fibriogen. A computer-assisted structural analysis of the rabbit FPA demonstrated that the Thr is located at the top of the N-termmal cluster, whereas the Thr in the chicken FPA exists in a linear and flexible peptide. Since the Thr on the chicken FPA seemed to fluctuate in the peptide, recognition of the Thr by habutobin might be unstable and ineffective. In conclusion, the exposure of Thr at position 10 in the FPA molecule is essential for habutobin-specific recognition of chicken fibrinogen.
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