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  • 1
    Online Resource
    Online Resource
    The disulphide bond pattern of bitistatin, a disintegrin isolated from the venom of the viper Bitis arietans
    Wiley ; 1997
    In:  FEBS Letters Vol. 416, No. 2 ( 1997-10-20), p. 197-202
    Details
    In: FEBS Letters, Wiley, Vol. 416, No. 2 ( 1997-10-20), p. 197-202
    Abstract: The disulphide bond pattern of the long disintegrin bitistatin (83 amino acids, 14 cysteines) was established using structural information gathered by amino acid analysis, N‐terminal sequencing, and molecular mass determination of fragments isolated by reversed‐phase HPLC after polypeptide degradation with trypsin and oxalic acid. A computer program was used to calculate all possible combinations of disulphide‐bonded peptides matching the mass spectrometric data, and the output was filtered using compositional and sequence data. Disulphide bonds between cysteines 16–34, 18–29, 28–51, 42–48, 47–72, and 60–79 are conserved in medium‐long disintegrins flavoridin and kistrin (70 amino acids, 12 cysteines), and the two cysteine residues at positions 5 and 24 found in bitistatin but not in other disintegrin molecules are disulphide‐bridged. This linkage creates an extra, large loop, which, depending on whether the NMR structure of flavoridin or kistrin is used for modelling the structure of bitistatin, lies opposite or nearly parallel, respectively, to the biologically active RGD‐containing loop.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(97)01203-9
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1997
    detail.hit.zdb_id: 1460391-3
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Biochemical and conformational characterisation of HSP‐3, a stallion seminal plasma protein of the cysteine‐rich secretory protein (CRISP) family
    Wiley ; 1997
    In:  FEBS Letters Vol. 420, No. 2-3 ( 1997-12-29), p. 179-185
    Details
    In: FEBS Letters, Wiley, Vol. 420, No. 2-3 ( 1997-12-29), p. 179-185
    Abstract: HSP‐3 is a member of the cysteine‐rich secretory protein (CRISP) family from stallion seminal plasma. We report a large‐scale purification protocol for native HSP‐3. This protein is a non‐glycosylated polypeptide chain with a p I of 8–9 and an isotope‐averaged molecular mass of 24 987±3 Da. The molecular mass of HSP‐3, determined by equilibrium sedimentation, is 26 kDa, showing that the protein exists in solution as a monomer. The concentration of HSP‐3 in the seminal plasma of different stallions ranged from 0.3 to 1.3 mg/ml. On average, 0.9–9 million HSP‐3 molecules/cell coat the postacrosomal and mid‐piece regions of an ejaculated, washed stallion spermatozoon, suggesting a role in sperm physiology. Conformational characterisation of purified HSP‐3 was assessed by combination of circular dichroism and Fourier‐transform infrared spectroscopies and differential scanning microcalorimetry. Based on secondary structure assignment, HSP‐3 may belong to the α+β class of proteins. Thermal denaturation of HSP‐3 is irreversible and follows a non‐two state transition characterised by a T m of 64°C, an enthalpy change of 75 kcal/mol, and a van 't Hoff enthalpy of 184 kcal/mol. Analysis of the spectroscopic and calorimetric data indicates the occurrence of aggregation of denatured HSP‐3 molecules and suggests the monomer as the cooperative unfolding unit.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(97)01514-7
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1997
    detail.hit.zdb_id: 1460391-3
    SSG: 12
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  • 3
    Online Resource
    Online Resource
    Primary Structure and Kinetic Interaction with Glycoproteins of The Lectin From Seeds of Cratylia Flor/Bunda
    Bentham Science Publishers Ltd. ; 1999
    In:  Protein & Peptide Letters Vol. 6, No. 1 ( 1999-02), p. 27-34
    Details
    In: Protein & Peptide Letters, Bentham Science Publishers Ltd., Vol. 6, No. 1 ( 1999-02), p. 27-34
    Abstract: The complete 236-amino-acid sequence of the glucose/mannose specific lectin from seeds of Cratylia floribunda (CFL) was determined by automated Edman sequencing of overlapping proteolytic peptides purified by HPLC after digestion of the lectin with endoproteinases Lys-C, Asp-N, trypsin and chymotrypsin. Mass spectrometry confirmed the sequence analysis and showed that CFL consists of a mixture of full length, single­ chain polypeptide (a-chain.-25397 ± 3 Da) and its• noncovalently associated p (residues 1-11 , 12847 ± 2 Da) and y (residues 119-236, 12568 ± 1 Da) fragments. The primary structure of Cratylia floribunda lectin has extensive amino acid sequence homology with those of lectins from species of the taxonomically related genera Canavalia and Dioclea. However, using surface plasmon resonance, CFL and ConA, the seed lectin from Canavalia ensiformis, displayed distinct kinetic interactions with glycoproteins, indicating structural differences in their extended glycan binding-sites.
    Type of Medium: Online Resource
    ISSN: 0929-8665
    URL: Article
    DOI: 10.2174/092986650601221107155254
    Language: English
    Publisher: Bentham Science Publishers Ltd.
    Publication Date: 1999
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  • 4
    Online Resource
    Online Resource
    Isolation and characterization of heparin‐ and phosphorylcholine‐binding proteins of boar and stallion seminal plasma. Primary structure of porcine pB1
    Wiley ; 1997
    In:  FEBS Letters Vol. 407, No. 2 ( 1997-04-28), p. 201-206
    Details
    In: FEBS Letters, Wiley, Vol. 407, No. 2 ( 1997-04-28), p. 201-206
    Abstract: In the bovine, seminal plasma heparin‐binding proteins bind to sperm lipids containing the phosphorylcholine group and mediate the capacitating effects of heparin‐like glycosaminoglycans during sperm residence in the female genital tract. We report the characterization of heparin‐ and phosphorylcholine‐binding proteins of stallion and boar seminal plasma. orse eminal lasma proteins HSP‐1 and HSP‐2, and boar protein pB1, belong to the same family as the bull heparin‐ and phosphorylcholine‐binding proteins BSP‐A 1/2 , BSP‐A 3 , and BSP‐30K. We have determined the amino acid sequence and posttranslational modifications of boar glycoprotein pB1. It contains 105 amino acids arranged into a mosaic structure consisting of a N‐terminal 18‐residue O ‐glycosylated polypeptide followed by two tandemly organized 40–45‐residue fibronectin type II domains. pB1 displays 60–65% amino acid sequence similarity with its equine and bovine homologues. However, in their respective seminal plasmas, the BSP and the HSP proteins associate into 90–150‐kDa oligomeric complexes, whereas pB1 forms a 35–40‐kDa complex with spermadhesin AQN‐1. In addition, pB1 appears to be identical to the recently described leukocyte adhesion regulator of porcine seminal fluid pAIF‐1. Our results tie in with the hypothesis that homologous proteins from different mammalian species may display distinct biological activities, which may be related to species‐specific aspects of sperm physiology.
    Type of Medium: Online Resource
    ISSN: 0014-5793 , 1873-3468
    URL: Article
    DOI: 10.1016/S0014-5793(97)00344-X
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 1997
    detail.hit.zdb_id: 1460391-3
    SSG: 12
    Location Call Number Limitation Availability
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    Online Resource
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