Detection of fragment genesis in the mass spectrometer: Amino acid sequence analysis by DADI/MIKE, linked scan and collisional activation mass spectrometry. 6—Peptides containing trifunctional amino acids

1982 ◽  
Vol 9 (4) ◽  
pp. 153-157 ◽  
Author(s):  
René Steinauer ◽  
Urs Peter Schlunegger
Keyword(s):  
Mass Spectrometry ◽  
Amino Acids ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Mass Spectrometer ◽  
Collisional Activation ◽  
Amino Acid Sequence Analysis

Amino Acid Sequence Analysis of Human S100A7 (Psoriasin) by Tandem Mass Spectrometry

1995 ◽  
Vol 217 (1) ◽  
pp. 257-263 ◽  
Author(s):  
D.M. Burgisser ◽  
G. Siegenthaler ◽  
T. Kuster ◽  
U. Hellman ◽  
P. Hunziker ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Amino Acid Sequence Analysis

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
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Bovine Milk ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amino Acid Sequence Analysis ◽  
Naturally Occurring ◽  
Localize Potential

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.

6-Pyruvoyl tetrahydropterin synthase from salmon liver: Amino acid sequence analysis by tandem mass spectrometry

1992 ◽  
Vol 182 (2) ◽  
pp. 953-959 ◽  
Author(s):  
Charles R. Hauer ◽  
Walter Leimbacher ◽  
Peter Hunziker ◽  
Frank Neuheiser ◽  
Nenad Blau ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Tandem Mass Spectrometry ◽  
Tandem Mass ◽  
Amino Acid Sequence Analysis

scholarly journals Molecular Characterization of a Secreted Enzyme with Phospholipase B Activity from Moraxella bovis

2001 ◽  
Vol 183 (22) ◽  
pp. 6717-6720 ◽  
Author(s):  
Jacinta L. Farn ◽  
Richard A. Strugnell ◽  
Peter A. Hoyne ◽  
Wojtek P. Michalski ◽  
Jan M. Tennent
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Amino Acid Sequence Analysis ◽  
Lipolytic Enzymes ◽  
Infectious Bovine Keratoconjunctivitis ◽  
Phospholipase B ◽  
Moraxella Bovis

ABSTRACT A candidate for a vaccine against infectious bovine keratoconjunctivitis (IBK) has been cloned and characterized fromMoraxella bovis. The plb gene encodes a protein of 616 amino acids (molecular mass of ∼65.8 kDa) that expresses phospholipase B activity. Amino acid sequence analysis revealed that PLB is a new member of the GDSL (Gly-Asp-Ser-Leu) family of lipolytic enzymes.

Sign in / Sign up

Export Citation Format

Share Document