Lysine estimation with the modified Udy-dye binding method in hexaploid wheat

Khan, Mujahid

doi:10.1007/bf01947274

Cited by 5 publications

(3 citation statements)

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“…In the brains of AD patients, normal tau is sequestered by AD P-tau which might result in a decrease in available normal tau for MT assembly. Under these conditions, even a small amount of hyperphosphorylated L-tubulin (presumably in a compromised functional state) might contribute signi¢cantly to the disassembly of MTs either directly or through tubulin^MAP interaction proposed previously [25]. If the hyperphosphorylated L-tubulin (X79535) belonged to the membrane pool, it would be hard to attribute any function, since this area of research remains unexplored.…”

Section: Discussionmentioning

confidence: 95%

“…L-Tubulin (X79535) is not a major isotype of Ltubulin in neurons. L-III-Tubulin, which is the predominant isotype in neurons, has been shown to be phosphorylated, whereas type II and type IV were not found to be phosphorylated [25]. Therefore, a slight decrease in the speci¢c isotype (X79535) in the 100 000Ug supernatant may remain undetected considering its relatively small contribution to this pool.…”

Section: Discussionmentioning

confidence: 99%

“…Of the various tubulin isotypes, L-III isotype was previously shown to be phosphorylated [22^24]. Although phosphorylation of L-III-tubulin does not a¡ect its polymerization into MTs, it inhibits the microtubule-associated protein (MAP)2-promoted MT assembly, suggesting that this post-translational modi¢cation might be involved in the regulation of MT assembly through tubulinM AP interaction [25].…”

Section: Introductionmentioning

confidence: 99%

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A pool of β‐tubulin is hyperphosphorylated at serine residues in Alzheimer disease brain

Vijayan

El-Akkad²,

Grundke‐Iqbal³

et al. 2001

FEBS Letters

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In Alzheimer disease (AD) brain, activities of protein phosphatase (PP)-2A/PP-1 which are known to be associated with microtubules are compromised and are probably a cause of neurofibrillary degeneration through hyperphosphorylation of microtubule proteins. In the present study, an increase of V V11 pmol phosphate/W Wg protein in 100 000U Ug pellet from AD compared with age-matched control brains was found. Tau protein, which is hyperphosphorylated in AD can only account for V V4 pmol phosphate/W Wg protein, suggesting the presence of non-tau hyperphosphorylated proteins in the diseased brain. Western blot analysis with phosphoserine antibodies revealed a V V54 kDa non-tau protein to be significantly hyperphosphorylated in AD compared with age-matched control cases in the particulate fraction. The V V54 kDa protein was purified by preparative sodium dodecyl sulfate^polyacrylamide gel electrophoresis and identified as L L-tubulin by immunolabeling with specific antibodies, mass spectrometry analysis and by Nterminal amino acid sequencing. The purified protein was hyperphosphorylated at serine residues in AD. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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Section: Discussionmentioning

confidence: 95%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A pool of β‐tubulin is hyperphosphorylated at serine residues in Alzheimer disease brain

Vijayan

El-Akkad²,

Grundke‐Iqbal³

et al. 2001

FEBS Letters

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Monitoring of Maillard reactions in soy products

Molnár-Perl

Pintér-Szakács

1986

Z Lebensm Unters Forch

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Chemical mechanism and the analytical methods suggested in the literature for the analysis of early Maillard reactions are summarised and critically evaluated. The applicability of our method for the measurement of the Maillard reactions - the soluble raffinose oligosaccharides and the basic amino groups of proteins - are illustrated by following early Maillard reactions in differently denaturated soya bean samples. The quantitative relations of Maillard reactions taking place in natural matrices could be clarified by monitoring both of the reactants by means of methods not requiring correction factors.

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