Reverse phase high performance liquid chromatograph for analysis of casein phosphopeptides /
acetonitrile over 49 minutes. Selected fragments of alpha
| Main Author: | |
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| Format: | Thesis eBook |
| Language: | English |
| Published: |
[Place of publication not identified] :
[publisher not identified] ;
1994.
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| Subjects: | |
| Online Access: | Link to OAKTrust copy |
| Summary: | acetonitrile over 49 minutes. Selected fragments of alpha acute resolution of casein peaks. Peaks were individually amino acid composition matching that of the phosphopeptide and beta casein were collected and further resolved using a attached to the silica) analytical column. By extending the calcium in caseins. casein could not be conclusively matched to any of the chromatography) was used to purify casein phosphopeptides. collected and submitted to amino acid analysis for composition determination. Analysis containing multiple confirmed that the peak from the digested beta casein was in discovered that casein phosphopeptides are partially fact one of the phosphopeptides responsible for binding of fragment found in beta casein. Peaks from the digested alpha gradient to 1 5-85% over 70 minutes, the C1 8 column provided Initially, sodium casemate was enzymatically digested with Milk intrinsically provides the essential calcium milk that make it a natural source of calcium, it was peaks were found to have a significant number of serine phosphopeptide fragments expected. However, several of the phosphorylated serine residues were compared to computer precipitation, preliminary purification was achieved using a requirements in the diet. Upon examining the components of residues. Protein sequence analysis via Edman degradation responsible for the bioavailability of calcium in milk. This reverse phase C-1 8 (containing octadecyl hydrocarbons reverse phase C-3 (containing propyl hydrocarbons attached to simulated casein phosphopeptides generated from the Specifically, reverse phase HPLC (high performance liquid study examined high performance liquid chromatography as a the peaks of the digested beta casein was found to have an the silica) analytical column with a gradient of 0-70% trypsin at pH 8.0 for 24 hours. Following a calcium University of Wisconsin Genetics User Group (UWGCG). One of viable method for purifying casein phosphopeptides. |
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| Item Description: | "Major subject: Food Science and Technology". Vita. |
| Physical Description: | ix, 65 leaves : illustrations ; 28 cm. Also available online. |
| Bibliography: | Includes bibliographical references. |