Document Detail


What befalls the proteins and water in a living cell when the cell dies?
MedLine Citation:
PMID:  17022374     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The solvency of solutes of varying molecular size in the intracellular water of freshly-killed Ehrlich carcinoma cells fits the same theoretical curve that describes the solvency of similar solutes in a 36% solution of native bovine hemoglobin--a protein found only in red blood cells and making up 97.3% of the red cell's total intracellular proteins. The merging of the two sets of data confirms the prediction of the AI Hypothesis that key intracellular protein(s) in dying cells undergo(es) a transition from: (1) one in which the polypeptide NHCO groups assume a fully-extended conformation with relatively strong power of polarizing and orienting the bulk-phase water in multilayers; to (2) one in which most of the polypeptide NHCO groups are engaged in alpha-helical and other "introvert" conformations (see below for definition) with much weaker power in polarizing-orienting multilayers of bulk-phase water. This concordance of the two sets of data also shows that what we now call native hemoglobin--supposedly denoting hemoglobin found in its natural state in living red blood cells--, in fact, more closely resembles the water-polarizing, and -orienting intracellular proteins in dead cells. Although in the dead Ehrlich carcinoma cells as well as in the 36% solution of native hemoglobin, much of the protein's polypeptide NHCO groups are engaged in alpha-helical and other "introvert" conformation (Perutz 1969; Weissbluth 1974), both systems produce a weak but nonetheless pervasive and "long-range" water polarization and orientation. It is suggested that in both the dead Ehrlich carcinoma ascites cells and in the 36% native bovine hemoglobin solution, enough polypeptide NHCO groups assume the fully-extended conformation to produce the weak but far-reaching multilayer water polarization and orientation observed.
Authors:
Gilbert N Ling; Ya-zhen Fu
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Physiological chemistry and physics and medical NMR     Volume:  37     ISSN:  0748-6642     ISO Abbreviation:  Physiol Chem Phys Med NMR     Publication Date:  2005  
Date Detail:
Created Date:  2006-10-06     Completed Date:  2006-11-01     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8502230     Medline TA:  Physiol Chem Phys Med NMR     Country:  United States    
Other Details:
Languages:  eng     Pagination:  141-58     Citation Subset:  IM    
Affiliation:
Damadian Foundation for Basic and Cancer Research, Melville, NY 11747, USA. gilbertling@dobar.org
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MeSH Terms
Descriptor/Qualifier:
Animals
Carcinoma, Ehrlich Tumor / metabolism,  pathology*
Cattle
Cell Death*
Extracellular Space / metabolism
Hemoglobins / chemistry*
Intracellular Space / metabolism
Mice
Mice, Inbred ICR
Models, Biological*
Peptides / chemistry
Protein Conformation
Water / metabolism*
Chemical
Reg. No./Substance:
0/Hemoglobins; 0/Peptides; 7732-18-5/Water

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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