Zobrazeno 1 - 10
of 13
pro vyhledávání: '"Henk J. Bak"'
Publikováno v:
Trends in Food Science & Technology. 4:16-21
Dietary proteins are broken down to free amino acids in three phases: in the gut lumen, at the brush border of the enterocyte and in the cytoplasm of the enterocyte. The digestion and/or absorption of di- and tripeptides is more rapid than that of an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a52ee940b3d4ee5a9f00ed56705a4508
https://doi.org/10.1016/s0924-2244(05)80006-8
https://doi.org/10.1016/s0924-2244(05)80006-8
Publikováno v:
European Journal of Biochemistry, 198(1), 1-6. Blackwell Publishing Ltd
The primary structure of an intracellular ribonuclease (RNase LX) from cultured tomato (Lycopersicon esculentum) cells has been determined. Previous studies have shown that the protein is located inside the tomato cells but outside the vacuoles and t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22fc79bd2a951977a3fabe4c00c1a621
https://research.rug.nl/en/publications/d3ee1084-5fc6-46ce-8a2f-5274d5760154
https://research.rug.nl/en/publications/d3ee1084-5fc6-46ce-8a2f-5274d5760154
Autor:
Jaap J. Beintema, Henk J. Bak
Publikováno v:
European Journal of Biochemistry, 169(2), 333-348. Blackwell Publishing Ltd
As a final step in the elucidation of the primary structure of subunit a of Panulirus interruptus hemocyanin (657 residues, M r 75696 excluding two copper ions and carbohydrate), the amino acid sequence of the largest fragment obtained by limited try
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::31fdda954071441f154990fbc4c01f62
https://doi.org/10.1111/j.1432-1033.1987.tb13616.x
https://doi.org/10.1111/j.1432-1033.1987.tb13616.x
Autor:
Anne Volbeda, M. D. Moore, Takayuki K. Nemoto, Toshiyuki Takagi, E. Yokota, Jaap J. Beintema, Nell M. Soeter, Hitoshi Nakashima, Austen Riggs, W. Schartau, Hans-Jürgen Schneider, Bernt Linzen, W. P. J. Gaykema, Henk J. Bak, Johan M. Vereijken, P. Q. Behrens, Wim G. J. Hol
Publikováno v:
Science, 229(4713), 519-524. AMER ASSOC ADVANCEMENT SCIENCE
Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. Comparison of the amino acid sequence data for seven different subunits of arthropod hemocyanins from crustaceans and chelicerates shows many h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::adb9452dba70678b9fad1eebf33653e5
https://research.rug.nl/en/publications/078e465a-89f2-417a-98e0-6dc465353708
https://research.rug.nl/en/publications/078e465a-89f2-417a-98e0-6dc465353708
Autor:
Ben Neuteboom, Peter A. Jekel, Nell M. Soeter, Henk J. Bak, Johan M. Vereijken, Jaap J. Beintema
Publikováno v:
FEBS Letters, 204(1), 141-144. Wiley
Hemocyanins are large multi-subunit copper proteins that transport oxygen in many arthropods and molluscs. The amino acid sequence of subunit a of Panulirus interruptus hemocyanin (657 residues) has been completed and fitted to the electron-density m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6accab7cc681be70f9ad675e2baadf05
https://doi.org/10.1016/0014-5793(86)81402-8
https://doi.org/10.1016/0014-5793(86)81402-8
Autor:
Nell M. Soeter, Henk J. Bak, J.J. Beintema, Johan M. Vereijken, W. P. J. Gaykema, Wim G. J. Hol
Publikováno v:
Nature. 309:23-29
For the first time, the three-dimensional structure of a member of the copper-containing class of oxygen-carrying proteins—the haemocyanins—has been determined. The structure of Panulirus interruptus haemocyanin at 3.2 A resolution shows that eac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::34ad25d0cef5753f55e6273629c678a4
https://doi.org/10.1038/309023a0
https://doi.org/10.1038/309023a0
Publikováno v:
European Journal of Biochemistry, 113(1), 151-157. Blackwell Publishing Ltd
After CNBr cleavage of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens, five peptides and free homoserine were isolated (see preceding paper in this journal). The amino acid sequences of the three smallest peptides, viz. CB3, CB4 and CB5,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::368a600f87cc958cfeec19db8bc42792
https://hdl.handle.net/11370/cce8c663-5cd7-470c-8aa5-3ae0a57eeb4a
https://hdl.handle.net/11370/cce8c663-5cd7-470c-8aa5-3ae0a57eeb4a
Publikováno v:
European Journal of Biochemistry. 178:403-412
The primary structure of subunit b of Panulirus interruptus hemocyanin has been derived from two digests (trypsin and CNBr) and, in some cases, with aid from the similarity with the sequence of subunit a. Differences between the amidation states of A
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a6da4fbd0c2b61d67622bb379deee37
https://doi.org/10.1111/j.1432-1033.1988.tb14464.x
https://doi.org/10.1111/j.1432-1033.1988.tb14464.x
Publikováno v:
Journal of Molecular Biology. 207:829-832
A high precision, two-dimensional study of oxygen and carbon monoxide binding to Panulirus interruptus hemocyanin has been carried out. Global data analysis of three types of experiments, probing the molecule in its various states of CO and O2ligatio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7817b403c1762d6b25458f7218a734bd
https://doi.org/10.1016/0022-2836(89)90248-9
https://doi.org/10.1016/0022-2836(89)90248-9
Publikováno v:
Invertebrate Oxygen Carriers ISBN: 9783540169437
The primary structure of the a chain of Panulirus interruptus hemocyanin (657 residues) has been completed except for one overlap that remains to be proven chemically, and two amide positions, Glx-372 and Asx-405, that are uncertain at this moment. B
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5ffa4f41022dc8ee89e411d04717d4f4
https://doi.org/10.1007/978-3-642-71481-8_27
https://doi.org/10.1007/978-3-642-71481-8_27