Related ArticlesDetermination of the casein content in bovine milk by 31P-NMR.
J Dairy Res. 2002 Aug;69(3):411-8
Authors: Belloque J, Ramos M
The relative proportion of caseins to total protein is a parameter that can be used to control the protein quality in standardised milk, an increasing tendency in dairy industries. 31P-NMR was used to analyse the casein content of milk, by the quantitation of the area under the resonances belonging to SerP, and using methylenediphosphonic acid as internal standard. This procedure yielded good results, as similar values of caseins were obtained from N Kjeldahl and NMR analysis for slightly heated milk samples. Heating at 95 degrees C for 15 min did not alter the casein content results. Casein content of raw, pasteurised and UHT milks (25.6 +/- 1.4, 26.4 +/- 1.8, 25.5 +/- 1.6 g casein/l milk, respectively), obtained by NMR, were not significantly different, giving an average of 25.8 +/- 1.6 g casein/l for bulk liquid milk. This work concluded that 31P-NMR could be used as an alternative method to determine casein in raw, pasteurised, dry and UHT milks.
[NMR paper] Diffusion of polyethyleneglycols in casein solutions and gels as studied by pulsed fi
Diffusion of polyethyleneglycols in casein solutions and gels as studied by pulsed field gradient NMR.
Related Articles Diffusion of polyethyleneglycols in casein solutions and gels as studied by pulsed field gradient NMR.
Magn Reson Imaging. 2005 Feb;23(2):347-8
Authors: Colsenet R, Soderman O, Mariette F
Molecular transport characterized by diffusion coefficients is a key feature of food processes and especially in dairy processes. Caseins represent 80% of the protein content in milk and are directly involved in the formation of dairy gels....
[NMR paper] Determination of molecular mobility of lyophilized bovine serum albumin and gamma-glo
Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state 1H NMR and relation to aggregation-susceptibility.
Related Articles Determination of molecular mobility of lyophilized bovine serum albumin and gamma-globulin by solid-state 1H NMR and relation to aggregation-susceptibility.
Pharm Res. 1996 Jun;13(6):926-30
Authors: Yoshioka S, Aso Y, Kojima S
PURPOSE: Feasibility of solid-state 1H NMR for determining the mobility of protein molecules in lyophilized cakes was considered. The mobility in...
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[NMR paper] Assignment and secondary-structure determination of monomeric bovine seminal ribonucl
Assignment and secondary-structure determination of monomeric bovine seminal ribonuclease employing computer-assisted evaluation of homonuclear three-dimensional 1H-NMR spectra.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles Assignment and secondary-structure determination of monomeric bovine seminal ribonuclease employing computer-assisted evaluation of homonuclear three-dimensional 1H-NMR spectra.
Eur J Biochem. 1995 Apr 15;229(2):494-502
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[NMR paper] NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Related Articles NMR studies of the structure and environment of the milk protein alpha-lactalbumin.
Basic Life Sci. 1990;56:231-53
Authors: Berliner LJ, Kaptein R, Koga K, Musci G
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[NMR paper] Exploring the dynamic information content of a protein NMR structure: comparison of a
Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_120x27.gif Related Articles Exploring the dynamic information content of a protein NMR structure: comparison of a molecular dynamics simulation with the NMR and X-ray structures of Escherichia coli ribonuclease HI.
Proteins. 1999 Jul 1;36(1):87-110
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