Occurrence of high molecular weight EGF complexes in human milk.

1989 ◽  
Vol 53 (4) ◽  
pp. 1043-1050 ◽  
Author(s):  
Norihiro AZUMA ◽  
Eri HESAKA ◽  
Shuichi KAMINOGAWA ◽  
Kunio YAMAUCHI
Keyword(s):  
Molecular Weight ◽  
Human Milk ◽  
High Molecular Weight

scholarly journals Digestion of the zinc in human milk, cow's milk and a commercial babyfood: some implications for human infant nutrition

1986 ◽  
Vol 55 (2) ◽  
pp. 209-217 ◽  
Author(s):  
Peter Blakeborough ◽  
Michael I. Gurr ◽  
Dallyn N. Salter
Keyword(s):  
Molecular Weight ◽  
Human Milk ◽  
High Molecular Weight ◽  
Stomach Contents ◽  
Human Infant ◽  
Soluble Form ◽  
Cow’S Milk ◽  
Low Molecular Weight ◽  
Cow's Milk ◽  
Molecular Weight Form

1. The digestion of zinc present in human milk, cow's milk and a commercial babyfood was compared, using the piglet as a model for the human infant.2. In piglets given human milk the pH of stomach contents was approximately 1 and 0.4 units lower than that of animals given respectively cow's milk and babyfood. The pH values of intestinal contents were approximately neutral and did not vary with the type of feed.3. Hard casein curds were present throughout the stomachs and small intestines of animals fed on cow's milk or babyfood and between 55 and 70% Zn in these digesta samples were recovered in an insoluble form by centrifugation. In contrast, little solid material was observed in the digesta of animals fed on human milk, and 57 and 93% respectively of the Zn in digesta were recovered in a soluble form in the stomach and small intestine.4. Soluble fractions prepared by centrifugation of digesta were analysed by filtration on Sephadex G-150. After any of the three feeds, soluble Zn in stomach contents was mainly in a low-molecular-weight form. In intestinal samples, however, Zn was present in low- and high-molecular-weight forms. Whilst there were similar amounts of Zn in the low-molecular-weight form in all samples, approximately three times as much of the total intestinal Zn was in a soluble high-molecular-weight form complexed to proteins in the animals fed on human milk compared with those fed on cow's milk or babyfood.5. Analysis of protein-bound soluble Zn in intestinal samples on SDS-polyacrylamide gels resulted in a similar pattern of proteins for all feeds. Results indicated that at least some of these proteins were derived from intestinal secretions of the piglet.6. Some implications of these results in respect of the mode of digestion of Zn and its biological availability to the human infant are discussed.

Analysis of High-Molecular-Weight Oligosaccharides from Human Milk by Liquid Chromatography and MALDI-MS

1999 ◽  
Vol 71 (17) ◽  
pp. 3755-3762 ◽  
Author(s):  
Berndt Finke ◽  
Bernd Stahl ◽  
Anja Pfenninger ◽  
Michael Karas ◽  
Hannelore Daniel ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Liquid Chromatography ◽  
Human Milk ◽  
High Molecular Weight ◽  
Maldi Ms

Detection of High-Molecular-Weight RNA in Particles from Human Milk

Science ◽  
1972 ◽  
Vol 175 (4021) ◽  
pp. 542-544 ◽  
Author(s):  
J. Schlom ◽  
S. Spiegelman ◽  
D. H. Moore
Keyword(s):  
Molecular Weight ◽  
Human Milk ◽  
High Molecular Weight

scholarly journals Occurrence of High Molecular Weight EGF Complexes in Human Milk

1989 ◽  
Vol 53 (4) ◽  
pp. 1043-1050
Author(s):  
Norihiro Azuma ◽  
Eri Hesaka ◽  
Shuichi Kaminogawa ◽  
Kunio Yamauchi
Keyword(s):  
Molecular Weight ◽  
Human Milk ◽  
High Molecular Weight

Microtubule motors and other maps

1990 ◽  
Vol 48 (3) ◽  
pp. 1-1
Author(s):  
Richard B. Vallee
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Cytoplasmic Dynein ◽  
Organelle Transport ◽  
Structural Components ◽  
Microtubule Associated Proteins ◽  
Microtubule Motors ◽  
Associated Proteins ◽  
The Subject ◽  
Intracellular Motility

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.

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