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Titolo:
Micro-method to isolate and purify amyloid proteins for chemical characterization
Autore:
Kaplan, B; Murphy, CL; Ratner, V; Pras, M; Weiss, DT; Solomon, A;
Indirizzi:
Univ Tennessee, Grad Sch Med, Human Immunol & Canc Program, Dept Med, Knoxville, TN 37920 USA Univ Tennessee Knoxville TN USA 37920 , Dept Med, Knoxville, TN 37920 USA Chaim Sheba Med Ctr, Heller Inst Med Res, Tel Hashomer, Israel Chaim ShebaMed Ctr Tel Hashomer Israel t Med Res, Tel Hashomer, Israel Bar Ilan Univ, Dept Life Sci, Ramat Gan, Israel Bar Ilan Univ Ramat Gan Israel n Univ, Dept Life Sci, Ramat Gan, Israel
Titolo Testata:
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
fascicolo: 1, volume: 8, anno: 2001,
pagine: 22 - 29
SICI:
1350-6129(200103)8:1<22:MTIAPA>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
POLYACRYLAMIDE-GEL ELECTROPHORESIS; PERFORMANCE LIQUID-CHROMATOGRAPHY; DODECYL-SULFATE; PREPARATIVE ELUTION; ALZHEIMERS-DISEASE; SEPARATED PROTEINS; MILLIGRAM AMOUNTS; AA AMYLOIDOSIS; LIGHT-CHAINS; PURIFICATION;
Keywords:
amyloid; AA amyloidosis; AL amyloidosis; ATTR amyloidosis; micro-purification; amino acid sequencing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Solomon, A Univ Tennessee, Grad Sch Med, Human Immunol & Canc Program, Dept Med, 1924Alcoa Highway, Knoxville, TN 37920 USA Univ Tennessee 1924 AlcoaHighway Knoxville TN USA 37920 20 USA
Citazione:
B. Kaplan et al., "Micro-method to isolate and purify amyloid proteins for chemical characterization", AMYLOID, 8(1), 2001, pp. 22-29

Abstract

The amyloidoses represent a heterogeneous group of disorders characterizedby the pathologic deposition as fibrils of at least 20 different precursormolecules. To establish definitively the specific type of amyloid protein contained in fibrillar deposits, such material must be extracted, purified,and subjected to amino acid sequence analysis. Heretofore the chemical identification of amyloid components has required gram quantities of tissue. Given the often-limited amounts of sample available, e.g., that derived fromdiagnostic needle biopsies, we have developed a micro-method to isolate and purify amyloid from minute tissue specimens. The procedure involves micro-extraction of the amyloid with subsequent purification by SDS-PA GE, electroblotting onto PVDF membranes, excision and elution of amyloid protein-related bands, and reversed phase HPLC. Chemical and immunologic studies of isolated amyloid components have demonstrated the purity achieved with this technique and have provided information on the molecular mass, heterogeneityand immunoreactivity of the amyloid. Further, using this methodology, if has been possible to obtain sufficient material for amino acid-sequencing and thus to establish unequivocally the chemical and molecular composition ofthe fibrillar deposits. Our microtechnique has clinical import and also isapplicable to analyses of the amyloid found in experimental small animal models of these disorders.

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Documento generato il 20/09/20 alle ore 07:41:23