Improved Phos-tag SDS-PAGE under neutral pH conditions for advanced protein phosphorylation profiling

PROTEOMICS ◽  
2010 ◽  
Vol 11 (2) ◽  
pp. 319-323 ◽  
Author(s):  
Eiji Kinoshita ◽  
Emiko Kinoshita-Kikuta
Keyword(s):  
Protein Phosphorylation ◽  
Neutral Ph ◽  
Sds Page ◽  
Ph Conditions

scholarly journals Improved Phos-tag SDS-PAGE under neutral pH conditions for advanced profiling of protein phosphorylation

2012 ◽  
Vol 56 (Suppl_1) ◽  
pp. s41-s44
Author(s):  
Emiko Kinoshita-Kikuta ◽  
Eiji Kinoshita ◽  
Tohru Koike
Keyword(s):  
Protein Phosphorylation ◽  
Neutral Ph ◽  
Sds Page ◽  
Ph Conditions

Influence of bend geometry on flow accelerated corrosion under neutral pH conditions

2021 ◽  
Vol 122 ◽  
pp. 105127
Author(s):  
P. Madasamy ◽  
M. Mukunthan ◽  
P. Chandramohan ◽  
T.V. Krishna Mohan ◽  
Andrews Sylvanus ◽  
...  
Keyword(s):  
Accelerated Corrosion ◽  
Neutral Ph ◽  
Ph Conditions ◽  
Flow Accelerated Corrosion

scholarly journals Synthesis and HNO Donating Properties of the Piloty's Acid Analogue Trifluoromethanesulphonylhydroxamic Acid: Evidence for Quantitative Release of HNO at Neutral pH Conditions

2018 ◽  
Vol 24 (29) ◽  
pp. 7330-7334 ◽  
Author(s):  
Sonya K. Adas ◽  
Vinay Bharadwaj ◽  
Yang Zhou ◽  
Jiuhong Zhang ◽  
Alexander J. Seed ◽  
...  
Keyword(s):  
Neutral Ph ◽  
Acid Analogue ◽  
Ph Conditions

Molecular Basis of Chemical Chaperone Effects of N-octyl-b-valienamine on Human b-glucosidase in Low/neutral pH Conditions

2010 ◽  
Vol 03 (04) ◽  
pp. 104-112 ◽  
Author(s):  
Hiroyuki Jo ◽  
Katsuyuki Yugi ◽  
Seiichiro Ogawa ◽  
Yoshiyuki Suzuki ◽  
Yasubumi Sakakibara
Keyword(s):  
Molecular Basis ◽  
Chemical Chaperone ◽  
Neutral Ph ◽  
Ph Conditions

scholarly journals Epimerization and Decomposition of Kojibiose and Sophorose by Heat Treatment under Neutral pH Conditions

2019 ◽  
Vol 66 (1) ◽  
pp. 1-9 ◽  
Author(s):  
Kazuhiro Chiku ◽  
Mami Wada ◽  
Haruka Atsuji ◽  
Arisa Hosonuma ◽  
Mitsuru Yoshida ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Neutral Ph ◽  
Ph Conditions

Possible Roles for Protein Phosphorylation in Platelet Responses

1979 ◽  
Author(s):  
R.J. Haslam ◽  
J.E.B. Fox ◽  
S.E. Salama ◽  
J.A. Lynham
Keyword(s):  
Cyclic Amp ◽  
Protein Phosphorylation ◽  
Protein Kinases ◽  
Platelet Function ◽  
Subcellular Fractionation ◽  
Human Platelets ◽  
Type I ◽  
Sds Page ◽  
Dependent Protein ◽  
32P Incorporation

The relationships between the phosphorylation of specific platelet polypeptides and platelet function were studied using washed human platelets labelled by preincubation with [32p] Pi. Platelet polypeptides were separated by SDS-PAGE and 32P incorporation into them determined by autoradiography. Whereas induction of platelet aggregation alone did not affect protein phosphorylation, induction of the release reaction increased 3P incorporation into several polypeptides (P75,P47,P40,P27,P20,P19), including the P-light chain of platelet myosin (P20). These changes were inhibited by drugs that blocked Ca2 movements and may be due to activation of Ca2+-dependent protein kinases. Compounds that inhibited platelet function by increasing cyclic AMP (e.g. PCE1) also suppressed these reactions but, in addition, increased phosphorylation of other polypeptides (P50,P49,P36,P24,P22). Type I and Type II cyclic AMP-dependent protein kinases were present in platelets and may mediate Che latter effects of cyclic AMP. Subcellular fractionation of 32p-labelled platelets that had been exposed to PCE1 showed that P24 was present in membranes that could take up Ca2+ by an ATP-dependent mechanism. Membranes from PCE1-treated platelets took up Ca2+ more rapidly than control membranes. Thus, the cyclic AMP-dependent phosphorylation of P24 may stimulate the removal of Ca2+ from platelet cytosol and suppress Ca2+-dependent phosphorylation reactions necessary for release of granule constituents.

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