Showing papers on "Sequence analysis published in 1970"
TL;DR: The complete amino acid sequence of bovine α-lactalbumin has been established by characterization of the tryptic, chymotryptic, and peptic peptides isolated from enzymic hydrolysates of the two unique fragments obtained on cleavage of S-aminoethyl-α-l lactalbumin with cyanogen bromide.
301 citations
TL;DR: Sequence analysis has been performed on 125 different oligonucleotides arising from the digestion of 16S rRNA with T1 ribonuclease and a preliminary study has been made of a large internal fragment.
Abstract: Sequence analysis has been performed on 125 different oligonucleotides arising from the digestion of 16S rRNA with T1 ribonuclease. A preliminary study has also been made of a large internal fragment.
74 citations
TL;DR: Comparison to the provisional sequences of other human κ Bence-Jones proteins has verified the concept that the NH2-terminal half of κ light chains is prone to variation in sequence whereas the COOH-Terminal half has a fixed sequence except for one hereditary variation.
48 citations
TL;DR: A regular repeat of hydrophobic residues as required by the inter-chain packing of a coiled-coil structure is indicated by the isolation and sequence analysis of two varieties of peptides arising from the C-terminus of tropomyosin.
27 citations
TL;DR: Compared to the reference λ chain Sh, Protein Bo has additional residues at four new positions (the NH2 terminus and positions 27a, 27b, and 27c) and lacks a residue at position 96 (des-96) and the calculated molecular weight of the monomeric form of Protein Bo is 22,982.
21 citations
TL;DR: The primaryructure of the variable region of the human λ Bence-Jones Protein Ha has been determined by sequence analysis of the tryptic and chymotryptic peptides and the primary structure of the constant region has been deduced by partial sequence analysis and by homology.
17 citations
TL;DR: The data reported here concern the sequence analysis of two series of tryptic peptides obtained by unlimited cleavage of the chains by p-toluene sulfonamido-phenylethyl chloromethyl ketone -trypsin and the second following limitation of trypsin cleavage to arginyl residues after modification of lysyl residues by trifluoracetylation.
Abstract: Alpha chains of human haptoglobin have been prepared from whole haptoglobin of genetic type Hp 2–1 purified from the ascites fluid of a single patient. Amino acid sequence analysis has been carried out on these light chains which represent the products α1S and α2(F,S) of the single genes Hp1S and Hp2(F,S), and are, respectively, 83 and 142 residues in length. The data reported here concern the sequence analysis of two series of tryptic peptides, one obtained by unlimited cleavage of the chains by p-toluene sulfonamido-phenylethyl chloromethyl ketone - trypsin, and the second following limitation of trypsin cleavage to arginyl residues after modification of lysyl residues by trifluoracetylation. The major technique for sequence analysis of these peptides was a modification of the p-dimethylaminonaphthalene-sulfonyl-Edman (dansyl-Edman) procedure employing a new thin-layer chromatographic separation of the dansyl-amino acids. The sequences of these tryptic peptides in conjunction with those of the chymotryp...
16 citations
TL;DR: The amino acid sequence of mung bean and sunflower cytochromes c have been determined on 3 y moles of pure cytochrome by using a combination of high voltage paper electrophoresis and sequence analysis by the Dansyl/Edman method.
Abstract: The amino acid sequence of mung bean and sunflower cytochromes c have been determined on 3 y moles of pure cytochrome by using a combination of high voltage paper electrophoresis and sequence analysis by the Dansyl/Edman method. These data have been compared with the wheat germ cytochrome c sequence. If the present potential of the method continues to be realised it is hoped to establish the major branches of a phylogenetic tree for the plant kingdom in the future.
4 citations