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RESEARCH PRODUCT
Onco-fetal/laminin-binding collagen from colon carcinoma: detection of new sequences.
A. AquinoL. BasiricòM.m. BoutillonI.p. MinafraMaria AndrioloM. VanderrestSalvatore Minafrasubject
Macromolecular SubstancesBiopsyMolecular Sequence DataBiophysicsSequence (biology)In-gel digestionBiochemistryMoleculeHumansElectrophoresis Gel Two-DimensionalTrypsinAmino Acid SequenceCyanogen BromideLaminin bindingMolecular BiologyGeneChromatography High Pressure LiquidFetusMolecular massSequence Homology Amino AcidChemistryCell BiologyMolecular biologyPeptide FragmentsElectrophoresisBiochemistryColonic NeoplasmsCollagendescription
We have recently identified an oncofetal-laminin binding collagen (OF/LB) composed of three alpha chains, with the apparent molecular mass of about 100 kDa each, but bearing different pI. One of the chains appears markedly acidic in a bidimensional electrophoretic system, where the NEPHGE is used as first dimension separating gel, while the two more basic chains have similar migration as alpha 1(III) and alpha 1(I) collagen chains, respectively. Sequence analyses have been performed on CNBr-peptides, derived from pepsinized triple helical molecules and on tryptic fragments obtained after in gel digestion of the acidic band. The research of sequence homology with computerized databases indicated that the acidic chain represents a gene product distinct from either type I, type III and other known collagen chains, while the identity of the other two chains remains to be fully determined.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1995-02-15 | Biochemical and biophysical research communications |