ABSTRACT
The primary structures of purple acid phosphatase and uteroferrin, two iron-binding glycoproteins isolated from beef spleen and porcine uterine fluids, respectively, have been examined by a combination of tandem mass spectrometry and classical Edman sequencing methods. Reported here are amino acid sequence data covering more than 90% of the primary structures for these two proteins. The sequence data reveal an unexpectedly high degree of homology, greater than 90%, for these two proteins.
Subject(s)
Acid Phosphatase/genetics , Metalloproteins/genetics , Spleen/enzymology , Uterus/metabolism , Amino Acid Sequence , Animals , Cattle , Female , Isoenzymes , Mass Spectrometry , Sequence Homology, Nucleic Acid , Swine , Tartrate-Resistant Acid PhosphataseABSTRACT
The amino acid sequence of a bacteriochlorophyll a-protein from the green photosynthetic bacterium Prosthecochloris aestuarii strain 2K has been determined. Use was made of a tentative sequence deduced from a 2.8-A electron density map of the protein to help locate sequenced peptides. The polypeptide chain consists of 366 amino acids. The identities of 5 amino acids that ligand to the magnesium atoms of 5 of the 7 bacteriochlorophyll molecules present in each subunit of the trimeric complex have been confirmed as histidines.
Subject(s)
Bacteria/analysis , Bacterial Proteins/analysis , Amino Acid Sequence , PhotosynthesisABSTRACT
Bovine and equine growth hormones were chemically modified with tetranitromethane, at pH 7.4 during 5 h and at pH 8.0 in the presence of 8 M urea during 1 h. a) Both hormones have very similar but not identical reactivities. b) The nitration of the reactive tyrosines and tryptophan residues at pH 7.4 produces no detectable changes in their immunological or somatotrophic activities. C) The nitration of all tyrosine residues in both hormones gives rise to a complete loss of somatographic activity with no alteration of the immunological activity.
