Abstract One major and two minor para-κ -casein components were isolated after rennin treatment from each of two genetic variants of κ -casein (A and B) by carboxy-methyl cellulose chromatography. Homocitrullin was present only in the minor components, while the major component was richer in lysine. The minor components were not present in para-κ -casein preparations not treated with urea. These findings indicate that the minor para-κ -casein components are produced by carbamylation of lysine with the cyanate formed in the urea solution. The homocitrullin-free para-κ -caseins A and B were identical as judged by polyacrylamide gel electrophoresis and amino acid analysis. Each contained 108 amino acid residues (molecular weight of about...
The pH-titration curves of caseins isolated from milk by different methods, using NaOH, Ba(OH)2, NH4...
Human milk K-casein was isolated from the acid-precipitated casein fraction on Sephadex G-200 and Mo...
The objective of this study was to investigate the impact of natural variations in aS1-casein and b-...
Abstract κ -Casein and related compounds were subjected to electrophoresis on polyacrylamide gels ...
Proteins of the casein complex of milk arouse considerable interest as the precursors of biologicall...
A comparison of the products obtained by two methods of fractionation of casein indicate that the me...
For many years casein was believed to be a homogenous protein. However, early work with fractional p...
In the present study the precipitation of casein from the various milk samples such as cow milk, goa...
Approximately 30% of the nitrogen of κ-casein was soluble at pH 4·7 after the protein had been treat...
The main object of this thesis was to specifically modify histidine residues in κ-casein and KA1 an...
Summary A complex chromatogram showing seven overlapping peaks was obtained from κ -casein by grad...
Lactic acid bacteria contain different cell-envelope proteinases responsible for hydrolysis of casei...
Para-k-Casein entsteht durch Hydrolyse des kappa-Caseins nach Zugabe proteolytischer Enzyme zur Milc...
Summary Addition of low concentrations of cysteine or mercaptoethanol to the concentrated urea solu...
AbstractHuman κ-casein was prepared from whole casein by successive hydroxyapatite and thiol-Sepharo...
The pH-titration curves of caseins isolated from milk by different methods, using NaOH, Ba(OH)2, NH4...
Human milk K-casein was isolated from the acid-precipitated casein fraction on Sephadex G-200 and Mo...
The objective of this study was to investigate the impact of natural variations in aS1-casein and b-...
Abstract κ -Casein and related compounds were subjected to electrophoresis on polyacrylamide gels ...
Proteins of the casein complex of milk arouse considerable interest as the precursors of biologicall...
A comparison of the products obtained by two methods of fractionation of casein indicate that the me...
For many years casein was believed to be a homogenous protein. However, early work with fractional p...
In the present study the precipitation of casein from the various milk samples such as cow milk, goa...
Approximately 30% of the nitrogen of κ-casein was soluble at pH 4·7 after the protein had been treat...
The main object of this thesis was to specifically modify histidine residues in κ-casein and KA1 an...
Summary A complex chromatogram showing seven overlapping peaks was obtained from κ -casein by grad...
Lactic acid bacteria contain different cell-envelope proteinases responsible for hydrolysis of casei...
Para-k-Casein entsteht durch Hydrolyse des kappa-Caseins nach Zugabe proteolytischer Enzyme zur Milc...
Summary Addition of low concentrations of cysteine or mercaptoethanol to the concentrated urea solu...
AbstractHuman κ-casein was prepared from whole casein by successive hydroxyapatite and thiol-Sepharo...
The pH-titration curves of caseins isolated from milk by different methods, using NaOH, Ba(OH)2, NH4...
Human milk K-casein was isolated from the acid-precipitated casein fraction on Sephadex G-200 and Mo...
The objective of this study was to investigate the impact of natural variations in aS1-casein and b-...