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Title Chemical keys to an understanding of life processes
Subject Biochemistry ; Nucleic acids; Proteins
Description Twenty Second Annual Frederick William Reynolds Lecture.
Creator Smith, Emil L., 1911-
Publisher Extension Division, University of Utah
Date 1958-01-13
Date Digital 2008-05-29
Type Text
Format image/jpeg
Digitization Specifications Original scanned on Epson Expression 10000XL flatbed scanner and saved as 400 ppi uncompressed tiff. Display images generated in PhotoshopCS and uploaded into CONTENTdm Aquisition Station.
Resource Identifier,564
Source LD5526.U8 n.s. v.49 no.11
Language eng
Relation Digital reproduction of "Chemical keys to an understanding of life processes," J. Willard Marriott Library Special Collections
Rights Digital Image Copyright University of Utah
Metadata Cataloger Seungkeol Choe; Ken Rockwell
ARK ark:/87278/s6c8277g
Setname uu_fwrl
Date Created 2008-07-29
Date Modified 2008-07-31
ID 319868
Reference URL

Page Metadata

Title Page19
Description CHEMICAL KEYS TO AN UNDERSTANDING OF LIFE PROCESSES 19 major dietary source of galactose, prevents the tissue damage. Thus, galactose, a normal and valuable constituent of the human diet, is toxic for an individual who does not have the enzymic equipment to deal with this substance. In this situation as well as in a number of others, it is now realized that "one man's food is another man's poison." Many studies of microorganisms, plants and animals have revealed specific mutations, spontaneous or produced experimentally, in which the formation of a normal and necessary enzyme is prevented. Among interesting examples of genetic changes in man are those which result in the formation of abnormal types of hemoglobins. Hemoglobin is the red protein present in blood cells which carries oxygen from the lungs to the tissues. There is a disorder, genetically determined, in which the cells contain a hemoglobin which differs in solubility and other properties from normal hemoglobin. Cells containing normal hemoglobin retain their normal shape when there is little oxygen available. Cells containing the abnormal hemoglobin undergo a change in shape, called sickling, in the absence of oxygen; hence the terms sickle cells and sickle cell anemia, since individuals possessing such cells suffer from an anemia caused by the fact that these abnormal cells do not live a normal life span. Investigations comparing normal hemoglobin and sickle cell hemoglobin have shown that the two protein molecules are almost identical. However, Ingram has very recently shown that the two types of hemoglobin differ in a single amino acid residue. Thus, a mutation inherited by normal genetic laws is reflected by a specific alteration in protein structure. Of the approximately seven hundred amino acid residues present in hemoglobin, only one residue appears to have been changed as a result of the genetic change, and this has produced a change in physical properties which may be deleterious to the individuals carrying the abnormal hemoglobin. These and similar studies with other abnormal hemoglobins have shown that genetic factors somehow modify the biosynthesis of a specific protein. The amino acid sequence of the normal protein is altered by replacement of one amino acid residue by another. Thus a mutation, presumably representing an alteration in nucleic acid structure, is reflected by a change in protein structure. This is about as direct evidence as we are likely to get from human studies concerning genetic influence on protein synthesis. Investigators in many
Format image/jpeg
Identifier 024-RNLT-SmithE_Page19.jpg
Source Original Manuscript: Chemical keys to an understanding of life processes by Emil L. Smith.
Setname uu_fwrl
Date Created 2008-07-29
Date Modified 2008-07-29
ID 319860
Reference URL