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Two different glycopeptides were isolated in high yield from a thermolytic digest of porcine fibrinogen. Edman analysis established their sequences as Val-Glu-Asn(CHO)-Lys and Val-Gly-Glu-Asn(CHO)-Arg. These sequences are nearly identical to the two human fibrinogen glycopeptides, Val-Glu-Asn(CHO)-Lys (γ-chain), and Met-Gly-Glu-Asn(CHO)-Arg (β-chain). The predominant carbohydrate moiety of both asialoglycopeptides was a biantennary oligosaccharide with a core α(1 → 6)-linked fucose as reported earlier (Da Silvaet al.(1994)Arch. Biochem. Biophys.312, 151–157). Both glycopeptides can be dansylated and used as sensitive substrates forFlavobacterium meningosepticumendo-β-N-acetylglucosaminidases F2and F3. Porcine fibrinogen represents the best source for substrates with this oligosaccharide type that can be reliably produced in multimicromole quantities.