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Reconstituted Micelle Formation Using Reduced, Carboxymethylated Bovine κ-Casein and Human β-Casein

Overview of attention for article published in The Protein Journal, September 2006
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Title
Reconstituted Micelle Formation Using Reduced, Carboxymethylated Bovine κ-Casein and Human β-Casein
Published in
The Protein Journal, September 2006
DOI 10.1007/s10930-006-9022-7
Pubmed ID
Authors

Satish M. Sood, Tim Lekic, Harbir Jhawar, Harold M. Farrell, Charles W. Slattery

Abstract

In milk, kappa-casein, a mixture of disulfide-bonded polymers, stabilizes and regulates the size of the unique colloidal complex of protein, Ca2+ and inorganic phosphate (Pi) termed the casein (CN) micelle. However, reduced, carboxymethylated bovine kappa-CN (RCM-kappa) forms fibrils at 37 degrees C and its micelle-forming ability is in question. Here, the doubly- and quadruply-phosphorylated human beta-CN forms and 1:1 (wt:wt) mixtures were combined with RCM-kappa at different beta/kappa weight ratios. Turbidity (OD(400 nm)) and a lack of precipitation up to 37 degrees C were used as an index of micelle formation. Studies were with 0, 5 and 10 mM Ca2+ and 4 and 8 mM Pi. The RCM-kappa does form concentration-dependent micelles. Also, beta-CN phosphorylation level influences micelle formation. Complexes were low-temperature reversible and RCM-kappa fibrils were seen. There appears to be equilibrium between fibrillar and soluble forms since the solution still stabilized after fibril removal. The RCM-kappa stabilized better than native bovine kappa-CN.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 28 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 28 100%

Demographic breakdown

Readers by professional status Count As %
Researcher 8 29%
Other 5 18%
Student > Ph. D. Student 2 7%
Student > Doctoral Student 2 7%
Student > Master 1 4%
Other 1 4%
Unknown 9 32%
Readers by discipline Count As %
Agricultural and Biological Sciences 7 25%
Biochemistry, Genetics and Molecular Biology 6 21%
Chemistry 2 7%
Computer Science 1 4%
Immunology and Microbiology 1 4%
Other 1 4%
Unknown 10 36%
Attention Score in Context

Attention Score in Context

This research output has an Altmetric Attention Score of 3. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 14 July 2018.
All research outputs
#8,533,995
of 25,371,288 outputs
Outputs from The Protein Journal
#163
of 639 outputs
Outputs of similar age
#30,679
of 89,586 outputs
Outputs of similar age from The Protein Journal
#1
of 4 outputs
Altmetric has tracked 25,371,288 research outputs across all sources so far. This one is in the 43rd percentile – i.e., 43% of other outputs scored the same or lower than it.
So far Altmetric has tracked 639 research outputs from this source. They receive a mean Attention Score of 3.7. This one is in the 31st percentile – i.e., 31% of its peers scored the same or lower than it.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 89,586 tracked outputs that were published within six weeks on either side of this one in any source. This one is in the 13th percentile – i.e., 13% of its contemporaries scored the same or lower than it.
We're also able to compare this research output to 4 others from the same source and published within six weeks on either side of this one. This one has scored higher than all of them