Milk proteins: the future

Milk Proteins ◽  
2008 ◽  
pp. 501-511
Author(s):  
Mike Boland
Keyword(s):  
Milk Proteins ◽  
2020 ◽  
pp. 715-730
Author(s):  
Mike Boland
Keyword(s):  

Milk Proteins ◽  
2014 ◽  
pp. 571-583 ◽  
Author(s):  
Mike J. Boland
Keyword(s):  

1961 ◽  
Vol 13 ◽  
pp. 29-41
Author(s):  
Wm. Markowitz
Keyword(s):  

A symposium on the future of the International Latitude Service (I. L. S.) is to be held in Helsinki in July 1960. My report for the symposium consists of two parts. Part I, denoded (Mk I) was published [1] earlier in 1960 under the title “Latitude and Longitude, and the Secular Motion of the Pole”. Part II is the present paper, denoded (Mk II).


1978 ◽  
Vol 48 ◽  
pp. 387-388
Author(s):  
A. R. Klemola
Keyword(s):  

Second-epoch photographs have now been obtained for nearly 850 of the 1246 fields of the proper motion program with centers at declination -20° and northwards. For the sky at 0° and northward only 130 fields remain to be taken in the next year or two. The 270 southern fields with centers at -5° to -20° remain for the future.


Author(s):  
Godfrey C. Hoskins ◽  
Betty B. Hoskins

Metaphase chromosomes from human and mouse cells in vitro are isolated by micrurgy, fixed, and placed on grids for electron microscopy. Interpretations of electron micrographs by current methods indicate the following structural features.Chromosomal spindle fibrils about 200Å thick form fascicles about 600Å thick, wrapped by dense spiraling fibrils (DSF) less than 100Å thick as they near the kinomere. Such a fascicle joins the future daughter kinomere of each metaphase chromatid with those of adjacent non-homologous chromatids to either side. Thus, four fascicles (SF, 1-4) attach to each metaphase kinomere (K). It is thought that fascicles extend from the kinomere poleward, fray out to let chromosomal fibrils act as traction fibrils against polar fibrils, then regroup to join the adjacent kinomere.


Author(s):  
Robert J. Carroll ◽  
Marvin P. Thompson ◽  
Harold M. Farrell

Milk is an unusually stable colloidal system; the stability of this system is due primarily to the formation of micelles by the major milk proteins, the caseins. Numerous models for the structure of casein micelles have been proposed; these models have been formulated on the basis of in vitro studies. Synthetic casein micelles (i.e., those formed by mixing the purified αsl- and k-caseins with Ca2+ in appropriate ratios) are dissimilar to those from freshly-drawn milks in (i) size distribution, (ii) ratio of Ca/P, and (iii) solvation (g. water/g. protein). Evidently, in vivo organization of the caseins into the micellar form occurs in-a manner which is not identical to the in vitro mode of formation.


Author(s):  
Nicholas J Severs

In his pioneering demonstration of the potential of freeze-etching in biological systems, Russell Steere assessed the future promise and limitations of the technique with remarkable foresight. Item 2 in his list of inherent difficulties as they then stood stated “The chemical nature of the objects seen in the replica cannot be determined”. This defined a major goal for practitioners of freeze-fracture which, for more than a decade, seemed unattainable. It was not until the introduction of the label-fracture-etch technique in the early 1970s that the mould was broken, and not until the following decade that the full scope of modern freeze-fracture cytochemistry took shape. The culmination of these developments in the 1990s now equips the researcher with a set of effective techniques for routine application in cell and membrane biology.Freeze-fracture cytochemical techniques are all designed to provide information on the chemical nature of structural components revealed by freeze-fracture, but differ in how this is achieved, in precisely what type of information is obtained, and in which types of specimen can be studied.


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