Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Dayle A. Sly"'
Publikováno v:
International Journal of Biochemistry. 7:639-642
1. 1. Human milk proteose-peptone fraction contained an average of 45% carbohydrate compared to about 11% carbohydrate present in the bovine milk fraction. 2. 2. The human milk proteose-peptone fraction contained Lactobacillus bifidus var. Penn. grow
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a8ab430eaefe11119eaec5c33d2de150
https://doi.org/10.1016/0020-711x(76)90105-1
https://doi.org/10.1016/0020-711x(76)90105-1
Publikováno v:
International Journal of Biochemistry. 7:203-206
1. 1. Human lactoferrin in the iron-saturated form was treated with pepsin at pH 3.0, and a fragment with a single iron-binding site was isolated in a 90% pure state. 2. 2. Its mol. wt was near 33,000. 3. 3. Its N-terminal residue was alanine, and it
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::27e7b388d7f973023e6263337d1c8bfc
https://doi.org/10.1016/0020-711x(76)90021-5
https://doi.org/10.1016/0020-711x(76)90021-5
Autor:
W. J. Wolf, Dayle Ann Sly
Publikováno v:
Archives of Biochemistry and Biophysics. 110:47-56
Ultracentrifugation resolved water-extractable soybean proteins into four fractions of 2S, 7S, 11S, and 15S. Chromatography on hydroxylapatite with potassium phosphate gradients (0.03–0.5 M) at pH 7.6 yielded four major fractions, A, B, C, and D. F
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::23f7ce22621b4ffd037b6ccdf2261058
https://doi.org/10.1016/0003-9861(65)90153-0
https://doi.org/10.1016/0003-9861(65)90153-0
Autor:
Dayle Ann. Sly, Walter J. Wolf
Publikováno v:
Journal of Chromatography A. 15:247-250
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b18ba630755317d57d831470419acf8
https://doi.org/10.1016/s0021-9673(01)82776-x
https://doi.org/10.1016/s0021-9673(01)82776-x
Publikováno v:
Biochimica et biophysica acta. 385(1)
Radioactive iodine-labeled iron-saturated human transferrin was shown to enter the cytosol of rabbit reticulocytes but not erythrocytes, and to be combined therein with a small “carrier” material not identical to the membrane transferrin receptor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::daa8784d977ee55c3e4644730486fe24
https://pubmed.ncbi.nlm.nih.gov/1125261
https://pubmed.ncbi.nlm.nih.gov/1125261
Publikováno v:
International journal of peptide and protein research. 8(3)
Human serum transferrin was fragmented by N-bromosuccinimide and reduction-alkylation. It was observed that there were at least two each of tryptophanyl-serine and tryptophanyl-aspartic acid, and one each of tryptophanyl-alanine and tryptophanyl-glut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2b2506fc7bb6be76842ac92d136eb891
https://pubmed.ncbi.nlm.nih.gov/1279084
https://pubmed.ncbi.nlm.nih.gov/1279084
