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A S Inglis

Publications and source records attributed to A S Inglis.

At least 37 records · Page 2Linked to original sources
PubMed1981

Comparison of the nucleotide sequence of cloned DNA coding for an apolipoprotein (apo VLDL-II) from avian blood and the amino acid sequence of an egg-yolk protein (apovitellenin I): equivalence of the two sequences.

We have compared the amino acid sequences of two low-molecular-weight avian apoproteins: apoVLDL-II from very low-density lipoproteins of hen plasma and apovitellenin I from hen egg yolk. The sequence of White Leghorn apoVLDL-II was derived from the nucleotide sequence of cloned apoVLDL-II DNA (Chan et al., 1980). The sequenator was used to determine the amino acid sequence of apovitellenin I from two breeds of hen (White Leghorn and Australorp). The sequences from the two breeds were not only identical, but they also completely matched the predicted sequence derived from the apoVLDL-II DNA sequence. The identity reported here establishes that this protein is transported intact from the blood to the egg yolk.

Amino Acid Sequence↗
PubMed1981

Composition and sequence studies show that A/duck/Ukraine/1/63 haemagglutinin (Hav7) belongs to the Hong Kong (H3) subtype.

The haemagglutinin chains HA1 and HA2 from the avian influenza virus A/duck/Ukraine/1/63 (Hav7, Neq2) have been subjected to amino acid analysis and N-terminal sequencing. Automated sequenator analysis of HA1 (40 cycles), after enzymic removal of the N-terminal pyroglutamic acid blocking group, and HA2 (43 cycles) showed that the Hav7 haemagglutinin closely resembled the human Hong Kong (H3) haemagglutinins including the presence of the characteristic extended 10 residue sequence at the N-terminus of HA1. These findings, together with the amino acid compositions for both chains, demonstrate that the Hav7 haemagglutinin is structurally similar to the Hong Kong (H3) haemagglutinins.

Amino Acid Sequence↗
PubMed1980

Amino acid sequence of cyanogen bromide fragment CN2 from Hong Kong influenza haemagglutinin heavy chain.

The amino acid sequence of cyanogen bromide peptide CN2 from the heavy chain (HA1) of the haemagglutinin of the Hong Kong variant A/Memphis/102/72 has been obtained by direct, automated sequence analysis on the whole fragment and by manual dansyl-Edman degradation of tryptic, peptic and chymotryptic peptides. It was found to contain 92 amino acid residues, including a large, insoluble, tryptic core peptide (residues 62-87). It did not contain any half-cystine residues or carbohydrate. The determination of its structure was complicated by the presence of an Asn-Ile bond at positions 48-49 which was readily cleaved by both trypsin and chymotrypsin.

Amino Acid Sequence↗
PubMed1980

N-terminal amino acid sequence of proalbumin from inbred buffalo rats.

The sequence of radioactively labelled amino acids at the N-terminus of proalbumin was determined by automated Edman-degradation. [3H] Valine, [3H]phenylalanine or [14C]arginine was incorporated into protein in vivo for a time period of 10 min after injection. Since albumin remains unlabelled during this time period (Urban et al., 1976), separation of proalbumin and albumin was not required for this work. Hence, compared to previous methods, a shorter purification procedure could be used which increased the yield of anti-albumin-precipitable protein and reduced the risk of proteolysis. Microsomes were prepared from livers removed 10 min after injection of the radioactively labelled amino acids. A buffer extract of the acetone-dried powder from these microsomes was chromatographed on DEAE-cellulose. All protein obtained after chromatography which could be precipitated with antiserum to serum albumin was isolated by immunoprecipitation and subsequent separation of the antigen-antibody complex. The sequence of radioactive amino acids in this antigen preparation suggests that about 20-25% of proalbumin possessed at the N-terminus the pentapeptide sequence X-Val-Phe-Arg-Arg- whereas 75-80% contained the hexapeptide sequence Arg-X-Val-Phe-Arg-Arg-.

Albumins↗
PubMed1978

Amino acid sequences of alpha-helical segments from S-carboxymethylkerateine-A. Complete sequence of a type-II segment.

1. The helical fragments obtained by partial chymotryptic digestion of S-carboxymethylkeratine-A, the low-sulphur fraction from wool, were fractionated into type-I and type-II helical segments in aqueous urea under conditions limiting carbamoylation. 2. The amino acid sequence of a 109-residue type-II segment was completed by using the sequenator. 3. When the data were incorporated into a helical model of 3.6 residues per turn the hydrophobic residues generated a band aligned at a slight angle to the helical axis. This result is in accord with the postulated coiled-coil structure of the crystalline regions of alpha-keratin.

Amino Acid Sequence↗
PubMed1978

Amino acid sequences of alpha-helical segments from S-carbosymethylkerateine-A. Complete sequence of a type-I segment.

The amino acid sequence of a type-I helical segment from the low-sulphur protein (S-carboxymethylkerateine-A) of wool was determined by combining automatic and manual-sequencing data. Whereas in the type-II helical segment most of the cationic groups occur in pairs, 11 of the 22 anionic residues in the sequence of the type-I segment were situated next to a second anionic residue. This suggests possible interactions between type-I and type-II helical segments in alpha-keratin. As observed with the sequence of a type-II helical segment a model constructed on 3.6 residues per turn of helix shows a line of hydrophobic residues along the helix, thereby supporting the physicochemical evidence that the molecule is predominantly helical and forms part of a coiled-coil structure. Examination of the sequence data by predictive methods indicates the possibilty of extensive sections of alpha-helix interspersed with discontinuities. The molecule contains a number of regions with peptide sequences identical with those found by other workers after enzymic digestion of fractions from oxidized wool.

Amides↗
PubMed1976

Synthesis of albumin via a precursor protein in cell suspensions from rat liver.

The mechanism of the biosynthesis of albumin was studied in cell suspensions from rat liver. The cells were prepared by continuous perfusion of the liver in situ with 0.05% collagenase and 0.10% hyaluronidase and incubated under conditions optimized for the incorporation of amino acids into protein. Seven minutes after starting the incubation L-[1-14C]leucine was added, followed after 25 min by a 15 or 30-min chase with an 830-fold excess of non-radioactive L-leucine. Total protein, an albumin-like protein, and albumin were isolated from samples withdrawn immediately of total protein was found to remain constant after addition of the non-radioactive L-leucine, whereas that of the albumin-like protein decreased and that of albumin increased with incubation time. The increase in albumin radioactivity accounted for the decrease in radioactivity of the albumin-like protein, suggesting that the latter is a precursor of albumin. The precursor protein differed from albumin by an oligopeptide extension at the N-terminal end.

Albumins↗
PubMed1976

Primary structure of apovitellenin I from hen egg yolk and its comparison with emu apovitellenin I.

The amino acid sequence of apovitellenin I from hen egg yolk has been determined using both automatic and manual procedures; it comprises 82 residues. Hen apovitellenin shows considerable homology with emu apovitellenin I which contains 84 residues. Besides two deletions in the sequence, the hen protein differs in 28 positions from the emu protein; 26 of these positions may have arisen from single base changes. The changes are largely conservative ones, which suggest that the structure and function have been preserved despite extensive mutation.

Amino Acid Sequence↗
PubMed1975

Rapid identification of amino acid derivatives from the sequenator.

A simple procedure is described for converting thiazolinones, from the protein sequenator, to the more stable phenylthiohydantoins without using the conventional HCI conversion procedure. The thiazolinones are applied to a silica gel plate and converted to phenylthiohydantoins by heating at 140 for 5-10 min, in the presence of heptafluorobutyric acid, prior to chromatography. After chromatography, measurements of the yields of the derivatives on the plate can be made with a variable-wave-length thin-layer chromatography scanner. This is shown to be a useful adjunct for identifications.

Amino Acid Sequence↗