Structural and functional relationship of red blood cell protein 4.1 to synapsin I

K. E. Krebs, S. M. Prouty, Ian Zagon, S. R. Goodman

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

It has been suggested that the neuron specific protein synapsin I is closely related to red blood cell (rbc) protein 4.1. A systematic comparison of the structural and functional properties of rbc protein 4.1 and synapsin I has been carried out. There is approximately a three order of magnitude difference in cross reactivity of synapsin I with rbc 4.1 antiserum vs. synapsin I antiserum, as determined by a competitive quantitative dot assay. Two-dimensional chymotryptic iodopeptide mapping analysis demonstrated limited peptide homology (~34% spot overlap) between rbc 4.1 and synapsin I. Dephosphorylated synapsin I binds saturably to brain spectrin (240/235) with an estimated dissociation constant (K(d)) of 700 nM and a maximal binding capacity of 4 mol synapsin I/mol spectrin tetramer, similar to the affinity and stoichiometry of 4.1 binding to rbc spectrin. Synapsin I was found to bind to the terminal ends of the brain spectrin tetramer by low-angle rotary shadowing, analogous to 4.1 binding to rbc spectrin. In summary, synapsin I is structurally and immunologically distinct from rbc 4.1, yet shares functional similarities with rbc 4.1 with respect to its spectrin binding characteristics.

Original languageEnglish (US)
JournalAmerican Journal of Physiology - Cell Physiology
Volume253
Issue number4
StatePublished - Dec 1 1987

Fingerprint

Synapsins
Blood Proteins
Spectrin
Erythrocytes
Immune Sera
Iodoproteins
Brain
Neurons

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology

Cite this

@article{9fee60ac97ce4fae929b7b64eae2cc87,
title = "Structural and functional relationship of red blood cell protein 4.1 to synapsin I",
abstract = "It has been suggested that the neuron specific protein synapsin I is closely related to red blood cell (rbc) protein 4.1. A systematic comparison of the structural and functional properties of rbc protein 4.1 and synapsin I has been carried out. There is approximately a three order of magnitude difference in cross reactivity of synapsin I with rbc 4.1 antiserum vs. synapsin I antiserum, as determined by a competitive quantitative dot assay. Two-dimensional chymotryptic iodopeptide mapping analysis demonstrated limited peptide homology (~34{\%} spot overlap) between rbc 4.1 and synapsin I. Dephosphorylated synapsin I binds saturably to brain spectrin (240/235) with an estimated dissociation constant (K(d)) of 700 nM and a maximal binding capacity of 4 mol synapsin I/mol spectrin tetramer, similar to the affinity and stoichiometry of 4.1 binding to rbc spectrin. Synapsin I was found to bind to the terminal ends of the brain spectrin tetramer by low-angle rotary shadowing, analogous to 4.1 binding to rbc spectrin. In summary, synapsin I is structurally and immunologically distinct from rbc 4.1, yet shares functional similarities with rbc 4.1 with respect to its spectrin binding characteristics.",
author = "Krebs, {K. E.} and Prouty, {S. M.} and Ian Zagon and Goodman, {S. R.}",
year = "1987",
month = "12",
day = "1",
language = "English (US)",
volume = "253",
journal = "American Journal of Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "4",

}

Structural and functional relationship of red blood cell protein 4.1 to synapsin I. / Krebs, K. E.; Prouty, S. M.; Zagon, Ian; Goodman, S. R.

In: American Journal of Physiology - Cell Physiology, Vol. 253, No. 4, 01.12.1987.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structural and functional relationship of red blood cell protein 4.1 to synapsin I

AU - Krebs, K. E.

AU - Prouty, S. M.

AU - Zagon, Ian

AU - Goodman, S. R.

PY - 1987/12/1

Y1 - 1987/12/1

N2 - It has been suggested that the neuron specific protein synapsin I is closely related to red blood cell (rbc) protein 4.1. A systematic comparison of the structural and functional properties of rbc protein 4.1 and synapsin I has been carried out. There is approximately a three order of magnitude difference in cross reactivity of synapsin I with rbc 4.1 antiserum vs. synapsin I antiserum, as determined by a competitive quantitative dot assay. Two-dimensional chymotryptic iodopeptide mapping analysis demonstrated limited peptide homology (~34% spot overlap) between rbc 4.1 and synapsin I. Dephosphorylated synapsin I binds saturably to brain spectrin (240/235) with an estimated dissociation constant (K(d)) of 700 nM and a maximal binding capacity of 4 mol synapsin I/mol spectrin tetramer, similar to the affinity and stoichiometry of 4.1 binding to rbc spectrin. Synapsin I was found to bind to the terminal ends of the brain spectrin tetramer by low-angle rotary shadowing, analogous to 4.1 binding to rbc spectrin. In summary, synapsin I is structurally and immunologically distinct from rbc 4.1, yet shares functional similarities with rbc 4.1 with respect to its spectrin binding characteristics.

AB - It has been suggested that the neuron specific protein synapsin I is closely related to red blood cell (rbc) protein 4.1. A systematic comparison of the structural and functional properties of rbc protein 4.1 and synapsin I has been carried out. There is approximately a three order of magnitude difference in cross reactivity of synapsin I with rbc 4.1 antiserum vs. synapsin I antiserum, as determined by a competitive quantitative dot assay. Two-dimensional chymotryptic iodopeptide mapping analysis demonstrated limited peptide homology (~34% spot overlap) between rbc 4.1 and synapsin I. Dephosphorylated synapsin I binds saturably to brain spectrin (240/235) with an estimated dissociation constant (K(d)) of 700 nM and a maximal binding capacity of 4 mol synapsin I/mol spectrin tetramer, similar to the affinity and stoichiometry of 4.1 binding to rbc spectrin. Synapsin I was found to bind to the terminal ends of the brain spectrin tetramer by low-angle rotary shadowing, analogous to 4.1 binding to rbc spectrin. In summary, synapsin I is structurally and immunologically distinct from rbc 4.1, yet shares functional similarities with rbc 4.1 with respect to its spectrin binding characteristics.

UR - http://www.scopus.com/inward/record.url?scp=0023515494&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023515494&partnerID=8YFLogxK

M3 - Article

VL - 253

JO - American Journal of Physiology

JF - American Journal of Physiology

SN - 0363-6143

IS - 4

ER -