Efficacy of the phosphorylation of synthetic peptides by purified catalytic subunit of PKA (PKAcat) from bovine lens depends on the amino acid sequence of the peptides

B. Samanta, G. Mező, K. P. Das, A. C. Ghose, F. Hudecz, P. C. Sen

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

Protein kinase (PK) A catalytic (PKAcat) subunit was purified to homogeneity from bovine lens using a 100-kDa cut-off membrane filtration followed by different chromatographic procedures. The molecular weight of PKAcat was found to be 41 kDa. The kinase phosphorylates histone IIIs and other synthetic modified peptides of VRKRTLRRL with different amino acid environment. The extent of phosphorylation depends not only on the presence of Ser or Thr (phosphorylating residues) but also on other surrounding amino acid residues. Although some peptides compete in phosphorylating histone, they are not very significant. The result suggests that the extent of phosphorylation depends on the amino acid residue(s) surrounding phosphorylable residue(s) on the peptide. Copyright Blackwell Munksgaard, 2005.

Original languageEnglish
Pages (from-to)445-449
Number of pages5
JournalJournal of Peptide Research
Volume65
Issue number4
DOIs
Publication statusPublished - Apr 2005

Fingerprint

Phosphorylation
Lenses
Amino Acid Sequence
Catalytic Domain
Amino Acids
Peptides
Protamine Kinase
Cyclic AMP-Dependent Protein Kinases
Histones
Molecular Weight
Molecular weight
Membranes

Keywords

  • Bovine lens
  • Phosphorylation
  • Protein kinase A catalytic subunit
  • Synthetic peptides

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology

Cite this

Efficacy of the phosphorylation of synthetic peptides by purified catalytic subunit of PKA (PKAcat) from bovine lens depends on the amino acid sequence of the peptides. / Samanta, B.; Mező, G.; Das, K. P.; Ghose, A. C.; Hudecz, F.; Sen, P. C.

In: Journal of Peptide Research, Vol. 65, No. 4, 04.2005, p. 445-449.

Research output: Contribution to journalArticle

@article{fe58e39a8ee24577aee09453b6ff4506,
title = "Efficacy of the phosphorylation of synthetic peptides by purified catalytic subunit of PKA (PKAcat) from bovine lens depends on the amino acid sequence of the peptides",
abstract = "Protein kinase (PK) A catalytic (PKAcat) subunit was purified to homogeneity from bovine lens using a 100-kDa cut-off membrane filtration followed by different chromatographic procedures. The molecular weight of PKAcat was found to be 41 kDa. The kinase phosphorylates histone IIIs and other synthetic modified peptides of VRKRTLRRL with different amino acid environment. The extent of phosphorylation depends not only on the presence of Ser or Thr (phosphorylating residues) but also on other surrounding amino acid residues. Although some peptides compete in phosphorylating histone, they are not very significant. The result suggests that the extent of phosphorylation depends on the amino acid residue(s) surrounding phosphorylable residue(s) on the peptide. Copyright Blackwell Munksgaard, 2005.",
keywords = "Bovine lens, Phosphorylation, Protein kinase A catalytic subunit, Synthetic peptides",
author = "B. Samanta and G. Mező and Das, {K. P.} and Ghose, {A. C.} and F. Hudecz and Sen, {P. C.}",
year = "2005",
month = "4",
doi = "10.1111/j.1399-3011.2005.00235.x",
language = "English",
volume = "65",
pages = "445--449",
journal = "Chemical Biology and Drug Design",
issn = "1747-0277",
publisher = "Blackwell",
number = "4",

}

TY - JOUR

T1 - Efficacy of the phosphorylation of synthetic peptides by purified catalytic subunit of PKA (PKAcat) from bovine lens depends on the amino acid sequence of the peptides

AU - Samanta, B.

AU - Mező, G.

AU - Das, K. P.

AU - Ghose, A. C.

AU - Hudecz, F.

AU - Sen, P. C.

PY - 2005/4

Y1 - 2005/4

N2 - Protein kinase (PK) A catalytic (PKAcat) subunit was purified to homogeneity from bovine lens using a 100-kDa cut-off membrane filtration followed by different chromatographic procedures. The molecular weight of PKAcat was found to be 41 kDa. The kinase phosphorylates histone IIIs and other synthetic modified peptides of VRKRTLRRL with different amino acid environment. The extent of phosphorylation depends not only on the presence of Ser or Thr (phosphorylating residues) but also on other surrounding amino acid residues. Although some peptides compete in phosphorylating histone, they are not very significant. The result suggests that the extent of phosphorylation depends on the amino acid residue(s) surrounding phosphorylable residue(s) on the peptide. Copyright Blackwell Munksgaard, 2005.

AB - Protein kinase (PK) A catalytic (PKAcat) subunit was purified to homogeneity from bovine lens using a 100-kDa cut-off membrane filtration followed by different chromatographic procedures. The molecular weight of PKAcat was found to be 41 kDa. The kinase phosphorylates histone IIIs and other synthetic modified peptides of VRKRTLRRL with different amino acid environment. The extent of phosphorylation depends not only on the presence of Ser or Thr (phosphorylating residues) but also on other surrounding amino acid residues. Although some peptides compete in phosphorylating histone, they are not very significant. The result suggests that the extent of phosphorylation depends on the amino acid residue(s) surrounding phosphorylable residue(s) on the peptide. Copyright Blackwell Munksgaard, 2005.

KW - Bovine lens

KW - Phosphorylation

KW - Protein kinase A catalytic subunit

KW - Synthetic peptides

UR - http://www.scopus.com/inward/record.url?scp=16844363307&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=16844363307&partnerID=8YFLogxK

U2 - 10.1111/j.1399-3011.2005.00235.x

DO - 10.1111/j.1399-3011.2005.00235.x

M3 - Article

C2 - 15813892

AN - SCOPUS:16844363307

VL - 65

SP - 445

EP - 449

JO - Chemical Biology and Drug Design

JF - Chemical Biology and Drug Design

SN - 1747-0277

IS - 4

ER -