A complementary radiopharmaceutical and mathematical model for quantitating hepatic-binding protein receptors

Kenneth Krohn, David R. Vera, Robert C. Stadalnik

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

Recent research in molecular biology has implicated cell surface glycoproteins, with their highly variable arrangements of sugar moieties, as the identifying markers that allow cells to uniquely distinguish individual chemical structures. The macromolecules which exhibit the property of recognition and binding of specific carbohydrate sequences are referred to as lectins.1 Carbohydrate-mediated recognition reactions allow more combinations of chemically unique receptor sites than are possible with polypeptides. While there are 20 common structural units in the latter case and only nine sugars, glycosidic bonds allow extensive structural branching that is unimportant in peptide bonding. The number of conceivable combinations and permutations of polypeptide structures is thus small compared to that for the highly branched oligosaccharides for which this number approaches 1024.

Original languageEnglish (US)
Title of host publicationReceptor Binding Radiotracers
PublisherCRC Press
Pages41-59
Number of pages19
Volume2
ISBN (Electronic)9781351358200
ISBN (Print)9781138506442
DOIs
StatePublished - Jan 1 2017
Externally publishedYes

Fingerprint

Radiopharmaceuticals
Theoretical Models
Peptides
Carbohydrate Sequence
Membrane Glycoproteins
Oligosaccharides
Molecular Biology
Carbohydrates
Research
hepatic sialoglycoprotein receptor

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Krohn, K., Vera, D. R., & Stadalnik, R. C. (2017). A complementary radiopharmaceutical and mathematical model for quantitating hepatic-binding protein receptors. In Receptor Binding Radiotracers (Vol. 2, pp. 41-59). CRC Press. https://doi.org/10.1201/9780203710548

A complementary radiopharmaceutical and mathematical model for quantitating hepatic-binding protein receptors. / Krohn, Kenneth; Vera, David R.; Stadalnik, Robert C.

Receptor Binding Radiotracers. Vol. 2 CRC Press, 2017. p. 41-59.

Research output: Chapter in Book/Report/Conference proceedingChapter

Krohn, Kenneth ; Vera, David R. ; Stadalnik, Robert C. / A complementary radiopharmaceutical and mathematical model for quantitating hepatic-binding protein receptors. Receptor Binding Radiotracers. Vol. 2 CRC Press, 2017. pp. 41-59
@inbook{19fad80a0c564345b48e4b5a1d8467fd,
title = "A complementary radiopharmaceutical and mathematical model for quantitating hepatic-binding protein receptors",
abstract = "Recent research in molecular biology has implicated cell surface glycoproteins, with their highly variable arrangements of sugar moieties, as the identifying markers that allow cells to uniquely distinguish individual chemical structures. The macromolecules which exhibit the property of recognition and binding of specific carbohydrate sequences are referred to as lectins.1 Carbohydrate-mediated recognition reactions allow more combinations of chemically unique receptor sites than are possible with polypeptides. While there are 20 common structural units in the latter case and only nine sugars, glycosidic bonds allow extensive structural branching that is unimportant in peptide bonding. The number of conceivable combinations and permutations of polypeptide structures is thus small compared to that for the highly branched oligosaccharides for which this number approaches 1024.",
author = "Kenneth Krohn and Vera, {David R.} and Stadalnik, {Robert C.}",
year = "2017",
month = "1",
day = "1",
doi = "10.1201/9780203710548",
language = "English (US)",
isbn = "9781138506442",
volume = "2",
pages = "41--59",
booktitle = "Receptor Binding Radiotracers",
publisher = "CRC Press",

}

TY - CHAP

T1 - A complementary radiopharmaceutical and mathematical model for quantitating hepatic-binding protein receptors

AU - Krohn, Kenneth

AU - Vera, David R.

AU - Stadalnik, Robert C.

PY - 2017/1/1

Y1 - 2017/1/1

N2 - Recent research in molecular biology has implicated cell surface glycoproteins, with their highly variable arrangements of sugar moieties, as the identifying markers that allow cells to uniquely distinguish individual chemical structures. The macromolecules which exhibit the property of recognition and binding of specific carbohydrate sequences are referred to as lectins.1 Carbohydrate-mediated recognition reactions allow more combinations of chemically unique receptor sites than are possible with polypeptides. While there are 20 common structural units in the latter case and only nine sugars, glycosidic bonds allow extensive structural branching that is unimportant in peptide bonding. The number of conceivable combinations and permutations of polypeptide structures is thus small compared to that for the highly branched oligosaccharides for which this number approaches 1024.

AB - Recent research in molecular biology has implicated cell surface glycoproteins, with their highly variable arrangements of sugar moieties, as the identifying markers that allow cells to uniquely distinguish individual chemical structures. The macromolecules which exhibit the property of recognition and binding of specific carbohydrate sequences are referred to as lectins.1 Carbohydrate-mediated recognition reactions allow more combinations of chemically unique receptor sites than are possible with polypeptides. While there are 20 common structural units in the latter case and only nine sugars, glycosidic bonds allow extensive structural branching that is unimportant in peptide bonding. The number of conceivable combinations and permutations of polypeptide structures is thus small compared to that for the highly branched oligosaccharides for which this number approaches 1024.

UR - http://www.scopus.com/inward/record.url?scp=85053341477&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85053341477&partnerID=8YFLogxK

U2 - 10.1201/9780203710548

DO - 10.1201/9780203710548

M3 - Chapter

AN - SCOPUS:85053341477

SN - 9781138506442

VL - 2

SP - 41

EP - 59

BT - Receptor Binding Radiotracers

PB - CRC Press

ER -