Periodate oxidation of biopolymers

Chatterjee, A. K.; Durant, G. J.; Hendrickson, H. R.; Lee, Y.C.; Montgomery, Rex

doi:10.1016/0006-291x(61)90302-3

Cited by 23 publications

(6 citation statements)

References 8 publications

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“…Reduction and alkylation under denaturing conditions destroys most of the conformation and antigenicity of native laminin (22) and also abolishes cell-binding activity. Periodate may have produced a similar effect by oxidizing disulfide bridges (23). Thus the data observed are consistent with the interpretation that the cells interact with a special three-dimensional arrangement of the peptide chains of laminin.…”

Section: Spreading Of Rat Hepatocytes On Lamininsupporting

confidence: 80%

Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins.

Johansson

Kjellén

Höök

et al. 1981

The Journal of Cell Biology

155

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In previous studies rat hepatocytes have been shown to adhere to substrates composed of collagen or fibronectin. In the present communication, the basement membrane protein laminin is reported to mediated the attachment and spreading of hepatocytes. The cell attachment-mediating activity of laminin was compared with that of fibronectin. The activity of fibronectin was heat sensitive, whereas laminin retained its activity after boiling. On the other hand, reduction and alkylation or periodate oxidation of the proteins affected only the cell attachment activity of laminin. Preincubation of cells with soluble fibronectin inhibited initial cell attachment to fibronectin but not to laminin substrates, and, reversely, soluble laminin selectively inhibited cell attachment to laminin. These results suggest that attachment of cells to substrates of the two proteins involves different cellular receptors recognizing distinct and nonidentical structures in the proteins.

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Section: Spreading Of Rat Hepatocytes On Lamininsupporting

confidence: 80%

Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins.

Johansson

Kjellén

Höök

et al. 1981

The Journal of Cell Biology

155

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“…We report also the results of the periodate oxidation of a purified glycopeptide. Two groups of workers (Bragg & Hough, 1961; Chatterjee, Durant, Lee & Montgomery, 1961) have applied this technique to an investigation of the structure of the carbohydrate by using whole egg albumin. However, since the protein is oxidized by periodate, these studies have been of limited value.…”

Section: (Received 2 October 1962)mentioning

confidence: 99%

Carbohydrates in protein. 5. Procedures for the isolation of glycopeptides from hen's-egg albumin and their oxidation by periodate

Fletcher¹,

Marks²,

Marshall³

et al. 1963

Biochemical Journal

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Vol. 87 DOCOSAHEXAENOIC ACID IN OX RETINA 265 of the cyclohexyl esters of the acids produced showed cyclohexyl propionate, dicyclohexyl malonate and dicyclohexyl succinate to be present, the last two in a 5-2: 1 molar ratio (calculated from the areas under the peaks on the chromatogram). Six structures are therefore possible for the docosahexaenoic acid: the double bonds could be at positions 4,7,

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“…Oxidation in the presence of ammonia gave the quinazoline (56) previously identified (338) as a photooxidation product of tryptophan. By contrast, indole-3- (56) propionic acid, the de-cx-amino analogue of tryptophan, was readily oxidized by sodium periodate in aqueous methanolic solution to give the acid (57) in 68% yield (78). When indole-3-propionyl-glycine was OC OCH2CH2COOH HCHO (57) oxidized under similar conditions, partial cleavage of the peptide bond occurred and free glycine was detected (18).…”

Section: Miscellaneous Oxidationsmentioning

confidence: 93%

“…Yields ofisolated products were low due to occurrence of deamination and tar formation (78). Products detected (8% yield) include formylkynurenine under neutral conditions and dioxindolylalanine under acid conditions.…”

Section: Miscellaneous Oxidationsmentioning

confidence: 97%