Disulphide arrangement in bovine caseins: localization of intrachain disulphide bridges in monomers of κ- and αs2-casein from bovine milk

1994 ◽  
Vol 61 (4) ◽  
pp. 485-493 ◽  
Author(s):  
Lone K. Rasmussen ◽  
Peter Højrup ◽  
Torben E. Petersen

SummaryNaturally occurring monomeric κ-casein and αs2-casein in bovine milk were purified by ion-exchange chromatography in order to localize potential intrachain disulphide bridges. Enzymic cleavage of the proteins followed by mass spectrometry and amino acid sequence analysis of cystine-containing peptides revealed the presence of an intrachain disulphide bond in both proteins.

1995 ◽  
Vol 217 (1) ◽  
pp. 257-263 ◽  
Author(s):  
D.M. Burgisser ◽  
G. Siegenthaler ◽  
T. Kuster ◽  
U. Hellman ◽  
P. Hunziker ◽  
...  

1992 ◽  
Vol 182 (2) ◽  
pp. 953-959 ◽  
Author(s):  
Charles R. Hauer ◽  
Walter Leimbacher ◽  
Peter Hunziker ◽  
Frank Neuheiser ◽  
Nenad Blau ◽  
...  

2020 ◽  
Vol 85 (3) ◽  
pp. 626-629
Author(s):  
Hisashi Muramatsu ◽  
Hiroki Maguchi ◽  
Taisuke Harada ◽  
Takehiro Kashiwagi ◽  
Chul-Sa Kim ◽  
...  

ABSTRACT Here, we report the identification of the gene encoding a novel enzyme, 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid desulfhydrase, in Burkholderia sp. HME13. The enzyme converts 3-(5-oxo-2-thioxoimidazolidin-4-yl) propionic acid and H2O to 3-(2,5-dioxoimidazolidin-4-yl) propionic acid and H2S. Amino acid sequence analysis of the enzyme indicates that it belongs to the DUF917 protein family, which consists of proteins of unknown function.


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