Evidence for novel linkages in a glycoprotein involving beta-hydroxyphenylalanine and beta-hydroxytyrosine
| Autor: | Tzong-Shin Lin, Pappachan E. Kolattukudy |
|---|---|
| Rok vydání: | 1976 |
| Předmět: |
Cutinase
D-Amino-Acid Oxidase Stereochemistry Hydrolases Phenylalanine Biophysics Biochemistry Serine Fusarium Tyrosine Threonine Amino Acids Molecular Biology Glycoproteins Alanine chemistry.chemical_classification Binding Sites Cell Biology Amino acid Enzyme chemistry Amino Acid Oxidoreductases Chromatography Thin Layer Hydroxy Acids Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 72(1) |
| ISSN: | 0006-291X |
| Popis: | Cutinase, an extracellular enzyme from Fusarium solani f. pisi contains about 4% covalently attached carbohydrates. Treatment of the enzyme with alkali resulted in β-elimination and generation of dehydroamino acids absorbing at 241 nm. NaB3H4 treatment in 0.1 N KOH followed by hydrolysis of the labeled protein gave rise to tritiated alanine, α-aminobutyric acid, phenylalanine, and tyrosine. Chemical and enzymatic degradation of the labeled phenylalanine showed that this amino acid was a 1:1 mixture of D- and L-stereo-isomers and that3H was equally distributed between the α- and β-positions. Therefore it is concluded that this glycoprotein contained 0-glycosidic linkages not only at serine and threonine residues but also at β-hydroxyphenylalanine and β-hydroxytyrosine; the latter two have not been found heretofore. |
| Databáze: | OpenAIRE |
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