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  • 1
    Electronic Resource
    Electronic Resource
    cDNA and protein sequence of a major pea seed albumin (PA 2 : Mr≈26 000) (1987)
    Springer
    Plant molecular biology 8 (1987), S. 37-45 
    Details
    ISSN: 1573-5028
    Keywords: amino acid sequence ; pea seed albumin ; internally repeated sequences
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Pea albumin 2 (PA2:Mr≈26000) is a major component of the albumin fraction derived from aqueous salt extracts of pea seed. Sodium dodecylsulfate-polyacrylamide gel electrophoresis and chromatography on DEAE-Sephacel resolve PA2 into two closely related components (PA2a and PA2b). A cDNA clone coding for one of these components has been sequenced and the deduced amino acid sequence compared with partial, chemically-determined sequences for cyanogen bromide peptides from both PA2 components. Complete amino acid sequences were obtained for the C-terminal peptides. The PA2 molecule of 230 amino acids contains four imperfect repeat sequences each of approximately 57 amino acids in length. The combined sequence data, together with a comparison of PA2-related polypeptides produced in vitro and in vivo, indicate that PA2 is synthesized without a signal sequence and does not undergo significant post-translational modification. Although both forms of PA2 contain Asn-X-Thr consensus sequences, neither form is glycosylated. Accumulation of PA2 contributes approximately 11% of the sulfur-amino acids in pea seeds (cysteine plus methionine equals 2.6 residues percent). Suppression of levels of PA2 polypeptides and their mRNAs in developing seeds of sulfur-deficient plants is less marked than that for legumin, in spite of the lower content of sulfur-amino acids in legumin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00016432
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    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
    Keywords: Trypsin inhibitor ; Kunitz-type inhibitor ; amino acid sequence ; winged bean ; Psophocarpus tetragonolobus (L.) DC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024626
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    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
    Keywords: Trypsin inhibitor ; Kunitz-type seed inhibitor ; amino acid sequence ; sequence similarity ; Leguminosae ; winged bean ; Psophocarpus tetragonolobus (L.) DC
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024782
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    Paper (German National Licenses)
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