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  • 1
    Digitale Medien
    Digitale Medien
    Amino acid sequence of the acidic kunitz-type trypsin inhibitor from winged-bean seed [Psophocarpus tetragonolobus (L.) DC] (1990)
    Springer
    The protein journal 9 (1990), S. 493-499 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Trypsin inhibitor ; Kunitz-type inhibitor ; amino acid sequence ; winged bean ; Psophocarpus tetragonolobus (L.) DC
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract The primary sequence of trypsin inhibitor-2 (WBTI-2) fromPsophocarpus tetragonolobus (L.) DC seeds was determined. This inhibitor consists of a single polypeptide chain of 182 amino acids, including four half-cystine residues, and an N-terminal residue of pyroglutamic acid. The sequence of WBTI-2 showed 57% identity to the basic trypsin inhibitor (WBTI-3) and 50% identity to the chymotrypsin inhibitor (WBCI) of winged bean, and 54% identity to the trypsin inhibitor DE-3 fromErythrina latissima seed. The similarity to the soybean Kunitz trypsin inhibitor (40%) and the other Kunitz-type inhibitors fromAdenanthera pavonina (30%) and wheat (26%) was much lower. Sequence comparisons indicate that thePsophocarpus andErythrina inhibitors are more closely related to each other than to other members of the Kunitz inhibitor family.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01024626
    Standort Signatur Erwartet Verfügbarkeit
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    Artikel (Nationallizenzen)
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  • 2
    Digitale Medien
    Digitale Medien
    Primary structure of kunitz-type trypsin inhibitor-2a (pI 5.9) fromPsophocarpus tetragonolobus (L.) DC seed (1991)
    Springer
    The protein journal 10 (1991), S. 183-188 
    Details
    ISSN: 1573-4943
    Schlagwort(e): Trypsin inhibitor ; Kunitz-type seed inhibitor ; amino acid sequence ; sequence similarity ; Leguminosae ; winged bean ; Psophocarpus tetragonolobus (L.) DC
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract The primary structure of acidic trypsin inhibitor-2a (WBTI-2a,pI 5.9) fromPsophocarpus tetragonolobus (L.) DC seed was determined. This inhibitor consists of a single polypeptide chain of 180 amino acids including four half-cystine residues and has an N-terminal residue of pyroglutamic acid. The sequence of WBTI-2a,pI 5.9, showed 84% identity to acidic trypsin inhibitor-2 (WBTI-2,pI 5.1) but only 57% identity to the basic trypsin inhibitor (WBTI-1,pI 8.9) and 50% identity to the chymotrypsin inhibitor of winged bean. The data indicate that winged bean seed contains a family of three Kunitz-type inhibitors which have about 50% identity.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01024782
    Standort Signatur Erwartet Verfügbarkeit
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    Artikel (Nationallizenzen)
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