Light Scattering, CD, and Ligand Binding Studies of Ferrihemoglobin-Polyelectrolyte Complexes (Record no. 44980)

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fixed length control field 02424nam a2200277Ia 4500
003 - CONTROL NUMBER IDENTIFIER
control field MX-MdCICY
005 - DATE AND TIME OF LATEST TRANSACTION
control field 20250625140637.0
040 ## - CATALOGING SOURCE
Transcribing agency CICY
090 ## - LOCALLY ASSIGNED LC-TYPE CALL NUMBER (OCLC); LOCAL CALL NUMBER (RLIN)
Classification number (OCLC) (R) ; Classification number, CALL (RLIN) (NR) B-10748
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245 10 - TITLE STATEMENT
Title Light Scattering, CD, and Ligand Binding Studies of Ferrihemoglobin-Polyelectrolyte Complexes
490 0# - SERIES STATEMENT
Volume/sequential designation BioPolymers, 50, p.153-161, 1999
520 3# - SUMMARY, ETC.
Summary, etc. Quasi-elastic light scattering (QELS), electrophoretic light scattering (ELS), CD spectroscopy, and azide binding titrations were used to study the complexation at pH 6.8 between ferrihemoglobin and three polyelectrolytes that varied in charge density and sign. Both QELS and ELS show that the structure of the soluble complex formed between ferrihemoglobin and poly(diallyldimethylammonium chloride)[PDADMAC]varies with protein concentration. At fixed 1.0 mg/mL polyelectrolyte concentration, protein addition increases complex size and decreases complex mobility in a tightly correlated manner. At 1.0 mg/mL or greater protein concentration, a stable complex is formed between one polyelectrolyte chain and many protein molecules (i.e., an intrapolymer complex)with apparent diameter approximately 2.5 times that of the protein-free polyelectrolyte. Under conditions of excess polyelectrolyte, each of the three ferrihemoglobin-polyelectrolyte solutions exhibits a single diffusion mode in QELS, which indicates that all protein molecules are complexed. CD spectra suggest little or no structural disruption of ferrihemoglobin upon complexation. Azide binding to the ferrihemoglobin-poly(2-acrylamide-2-methylpropanesulfonate)[PAMPS]complex is substantially altered relative to the polyelectrolyte-free protein, but minimal change is induced by complexation with an AMPS-based copolymer of reduced linear charge density. The change in azide binding induced by PDADMAC is intermediate between that of PAMPS and its copolymer
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element HEMOGLOBIN-POLYELECTROLYTE COMPLEXES
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element PROTEIN-POLYELECTROLYTE COMPLEXES
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element LIGHT SCATTERING
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element CD
650 14 - SUBJECT ADDED ENTRY--TOPICAL TERM
Topical term or geographic name entry element LIGAND BINDING
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Xia, J.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Dubin, P.L.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Kokufuta, E.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Havel, H.
700 12 - ADDED ENTRY--PERSONAL NAME
Personal name Muhoberac, B.B.
856 40 - ELECTRONIC LOCATION AND ACCESS
Uniform Resource Identifier <a href="https://drive.google.com/file/d/11Gzbfp0fHr_nl_0V_rK3iNdyTxJAeCgn/view?usp=drivesdk">https://drive.google.com/file/d/11Gzbfp0fHr_nl_0V_rK3iNdyTxJAeCgn/view?usp=drivesdk</a>
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Source of classification or shelving scheme Clasificación local
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  Clasificación local     Ref1 CICY CICY Documento préstamo interbibliotecario 25.06.2025   B-10748 25.06.2025 25.06.2025 Documentos solicitados