The Complete Amino Acid Sequence of Bovine α-Lactalbumin
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چکیده
منابع مشابه
The Complete Amino Acid Sequence of Bovine a-Lactalbumin*
The complete amino acid sequence of bovine oc-lactalbumin has been established. The unique seq,uence was deduced by characterization of the tryptic, chymotryptic, and peptic peptides isolated from enzymic hydrolysates of the two unique fragments obtained on cleavage of S-aminoethyl-a-lactalbumin with cyanogen bromide as described earlier. Important overlapping peptides were also obtained by seq...
متن کاملComparison of the amino acid sequence of bovine alpha-lactalbumin and hens egg white lysozyme.
hydride, was essentially the same as the release of unlabeled Nacetylgalactosaminitol from sialidase-treated OSM. These results suggest that the 14C-OSP contained the glycose units linked to polypeptide in the same manner as in the native OSM, i.e. to serine or threonine, or both. Numerous attempts to demonstrate this linkage directly by amino acid analysis before and after alkaline borohydride...
متن کاملTHE COMPLETE AMINO ACID SEQUENCE OF THE a-LACTALBUMIN FROM A MARSUPIAL
a-Lactalbumin was purified from a whey protein fraction of the milk of the red-necked wallaby (Macropus rufogrisem). The complete amino acid sequence was determined from the results of automatic sequenator analyses of the intact protein, the three cyanogen bromide fragments, and of peptides generated from the larger, COOH-terminal CNBr fragment by digestion with trypsin or staphylococcal protea...
متن کاملThe amino acid sequence of bovine adrenodoxin.
The preliminary amino acid sequence of bovine adrenodoxin previously reported from our laboratory has been shown to be in error. In the corrected sequence, adrenodoxin contains 114 amino acid residues. The residues Asx-GlxLeu in position ‘78, 79, and 80 and the aspartic acid residue in position 107 should be deleted from the previously reported sequence. The details of the primary structure det...
متن کاملThe Complete Amino Acid Sequence of Papain
The active cysteine of papain was labeled with W-iodoacetate and the cystine residues were reduced and coupled with unlabeled iodoacetate. The heptacarboxymethyl papain was then maleylated and hydrolyzed with trypsin. Key peptides were isolated from this hydrolysate which have permitted completion of the amino acid sequence of the protein. Thus, an earlier tentative and incomplete version of th...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)63827-5