American Society of Hematology

Fig. 4.

$Fig. 4. Determination of the cleavage sites in CTAP-III by gelatinase B. / After digestion of CTAP-III with gelatinase B, the reaction mixture was subjected to reverse-phase HPLC on a C8 column to separate the cleavage products into different fractions (top). Peptides were identified by aminoterminal sequencing and mass spectrometry analysis (bottom). Sequences in bold letters were determined by tandem MS/MS, and underlined sequences were determined by Edman degradation. Intact disulfide bridges (as determined by MS analysis) are indicated by lines between the cysteine pairs. The experimentally determined molecular mass of the fragments is compared with the calculated theoretical mass data. Positions of the cleavage sites are indicated by asterisks in the sequence of CTAP-III (lowest part of bottom panel). nd, not detectable.$

Determination of the cleavage sites in CTAP-III by gelatinase B.

After digestion of CTAP-III with gelatinase B, the reaction mixture was subjected to reverse-phase HPLC on a C8 column to separate the cleavage products into different fractions (top). Peptides were identified by aminoterminal sequencing and mass spectrometry analysis (bottom). Sequences in bold letters were determined by tandem MS/MS, and underlined sequences were determined by Edman degradation. Intact disulfide bridges (as determined by MS analysis) are indicated by lines between the cysteine pairs. The experimentally determined molecular mass of the fragments is compared with the calculated theoretical mass data. Positions of the cleavage sites are indicated by asterisks in the sequence of CTAP-III (lowest part of bottom panel). nd, not detectable.

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