scholarly journals Amino acid sequences around the disulphide bridges and methionine residues of porcine pepsin

1970 ◽  
Vol 118 (4) ◽  
pp. 611-623 ◽  
Author(s):  
J. Tang ◽  
B. S. Hartley
Keyword(s):  
Protein Structure ◽  
Amino Acid ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Disulphide Bridge ◽  
Porcine Pepsin ◽  
The Third ◽  
Acidic Residues ◽  
Methionine Residues

1. The amino acid sequences around three disulphide bridges and four methionine residues of porcine pepsin were studied by using diagonal electrophoresis methods. 2. Two of the three disulphide bridges were in small loops of five and six residues. The sequence around one of the two half-cystine residues of the third disulphide bridge had a large number of acidic residues. 3. The sequence of a tetrapeptide containing phosphoserine was also determined. 4. Four unique methionine-containing sequences were constructed. The information is sufficient for the determination of the overlaps in the cyanogen bromide fragments of pepsin. 5. The usefulness of diagonal methods in the study of protein structure, the relative positions of cystinyl and methionyl residues in porcine pepsin and the homology between pepsin and rennin are discussed.

scholarly journals Amino acid sequences around the cysteine residues of rabbit muscle triose phosphate isomerase

1971 ◽  
Vol 122 (2) ◽  
pp. 209-218 ◽  
Author(s):  
Janet C. Miller ◽  
S. G. Waley
Keyword(s):  
Amino Acid ◽  
Cyanogen Bromide ◽  
Triose Phosphate Isomerase ◽  
Amino Acid Sequences ◽  
Cysteine Residues ◽  
Rabbit Muscle ◽  
Amino Acid Residues ◽  
Triose Phosphate ◽  
Methionine Residues ◽  
Polypeptide Chains

1. The nature of the subunits in rabbit muscle triose phosphate isomerase has been investigated. 2. Amino acid analyses show that there are five cysteine residues and two methionine residues/subunit. 3. The amino acid sequences around the cysteine residues have been determined; these account for about 75 residues. 4. Cleavage at the methionine residues with cyanogen bromide gave three fragments. 5. These results show that the subunits correspond to polypeptide chains, containing about 230 amino acid residues. The chains in triose phosphate isomerase seem to be shorter than those of other glycolytic enzymes.

scholarly journals Studies On Reduced Wool Ix. The N-Terminal Sequence of A Fragment Produced by Cleavage of Component 8 With Cyanogen Bromide

1969 ◽  
Vol 22 (2) ◽  
pp. 471 ◽  
Author(s):  
IJ O'donnell
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Chemical Environment ◽  
Terminal Sequence ◽  
Terminal Residue ◽  
Amino Terminal ◽  
Fundamental Sequence ◽  
Methionine Residues

Component 8 is a major component extracted from reduced and carboxy-methylated wool. Further study of its reaction with cyanogen bromide and of the fractions obtained under carefully controlled disaggregating conditions has rev<\laled that while most of the methionine residues are in the same position relative to the ends of the chains, at least 30% of them appear to be in a different chemical environment from the rest. The evidence can be interpreted in terms of variations in some of the amino acids at particular points in a fundamental sequence of the 60 residues (CNBr3) at the amino terminal end. Further amino acid sequences near the acetylated terminal residue have been determined and provide examples of the amino acid variatioIl along the chain. One sequeIlce with variants is: N-acetyISer-(Tyr or Phe Or Pro)-Asp-(Phe or Leu)-SCMCySH-Leu-Pro-Asp-Leu-Ser-Phe-Arg-. There is a region in component 8 where many of the S-carboxymethylcysteine residues are congregated.

scholarly journals Amino Acid Sequence Studies on Sheep Liver Fructose-bisphosphatase. II The Complete Sequence

1983 ◽  
Vol 36 (3) ◽  
pp. 235 ◽  
Author(s):  
WK Fisher ◽  
EOP Thompson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Fructose Bisphosphatase ◽  
Proteolytic Digestion ◽  
Sheep Liver ◽  
Methionine Residues

The cyanogen bromide fragments of S-carboxymethylated fructose-bisphosphatase were purified. The amino acid sequences of the small fragments were determined by the dansyl-Edman method. The large fragments were subjected to proteolytic digestion to give smaller peptides more amenable for purification and sequencing by similar methods. Enzyme digests of the S-carboxymethylated enzyme gave overlap peptides containing the methionine residues.

Amino acid sequence of penicillopepsin. II. Isolation and characterization of thermolytic peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 885-894 ◽  
Author(s):  
Leticia Rao ◽  
Theo Hofmann
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Active Site ◽  
Amino Acid Sequences ◽  
Porcine Pepsin ◽  
Isolation And Characterization

The determination of the amino acid sequences of 70 peptides obtained from a thermoiytic digest of penicillopepsin (EC 3.4.23.7) is described. Fifty-six unique sequences ranging from 2 to 13 amino acids were compiled. Among these was a heptapeptide whose sequence is nearly identical with that of the epoxide-reactive active site peptide of porcine pepsin (EC 3.4.23.1). Considering unrecognized overlaps, a minimum of 272 and a maximum of 293 unique amino acids have been obtained. They account for about 90% of the amino acids of the enzyme.

Amino acid sequence of penicillopepsin. III. Isolation and characterization of amino terminal, tryptic, and tryptophanyl peptides

1976 ◽  
Vol 54 (10) ◽  
pp. 895-901
Author(s):  
C. Ian Harris ◽  
Leticia Rao ◽  
Paul Shutsa ◽  
Alexander Kurosky ◽  
Theo Hofmann
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Amino Acid Sequences ◽  
Affinity Column ◽  
Amino Terminal ◽  
Tryptic Digest ◽  
The Third ◽  
Isolation And Characterization

The amino acid sequences of peptides isolated from a tryptic digest of penicillopepsin (EC 3.4.23.7), a subtilisin (EC 3.4.21.14) digest of maleylated penicillopepsin, and a chymotryptic digest of penicillopepsin modified with dinitrophenylsulfenyl (DNPS) chloride have been determined. The first two digests identified four of the five lysyl residues of the enzyme as well as the N-terminal peptide. The third digest provided overlaps at three of the tryptophanyl residues. The DNPS-tryptophan peptides were isolated on an affinity column prepared by coupling dinitrophenyl antibody raised in sheep to cyanogen bromide-activated Sepharose.

Amino acid sequence of cyanogen bromide fragment CB3 of hog pepsin

1981 ◽  
Vol 46 (3) ◽  
pp. 655-666
Author(s):  
Ladislav Morávek ◽  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Cyanogen Bromide ◽  
Methionine Residues ◽  
Cyanogen Bromide Fragment

On the basis of the knowlidge of thermolytic, chymotryptic and substilisin peptides the amino acid sequence was determined of cyanogen bromide fragment CB3 representing the region between methionine residues I and II of pepsin: Thr-Gly-Ile-Leu-Gly-Tyr-Asp-Thr-Val-Gln-Val-Gly-Gly-Ile-Ser-Asp-Thr-Asn-Gln-Ile-Phe-Gly-Leu-Ser-Glu-Thr-Glu-Pro-Gly-Ser-Phe-Leu-Tyr-Tyr-Ala-Pro-Phe-Asp-Gly-Ile-Leu-Gly-Leu-Ala-Tyr-Pro-Ser-Ile-Ser-Ala-Ser-Gly-Ala-Thr-Pro-Val-Phe-Asp-Asn-Leu-Trp-Asp-Gln-Gly-Leu-Val-Ser-Gln-Asp-Leu-Phe-Ser-Val-Tyr-Leu-Ser-Ser-Asn-Asp-Asp-Ser-Gly-Ser-Val-Val-Leu-Leu-Gly-Gly-Ile-Asp-Ser-Ser-Tyr-Tyr-Thr-Gly-Ser-Leu-Asn-Trp-Val-Pro-Val-Ser-Val-Glu-Gly-Tyr-Trp-Gln-Ile-Thr-Leu-Asp-Ser-Ile-Thr-Met.

scholarly journals A novel giant secretion polypeptide in Chironomus salivary glands: implications for another Balbiani ring gene.

1985 ◽  
Vol 101 (3) ◽  
pp. 1044-1051 ◽  
Author(s):  
W Y Kao ◽  
S T Case
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Salivary Glands ◽  
Cyanogen Bromide ◽  
Tryptic Peptide ◽  
Amino Acid Sequences ◽  
The Other ◽  
Balbiani Ring ◽  
Sequence Organization ◽  
Peptide Maps

Chironomus salivary glands contain a family of high Mr (approximately 1,000 X 10(3)) secretion polypeptides thought to consist of three components: sp-Ia, sp-Ib, and sp-Ic. The use of a new extraction protocol revealed a novel high Mr component, sp-Id. Results of a survey of individual salivary glands indicated that sp-Id was widespread in more than a dozen strains of C. tentans and C. pallidivittatus. Sp-Id was phosphorylated at Ser residues, and a comparison of cyanogen bromide and tryptic peptide maps of 32P-labeled polypeptides suggested that sp-Ia, sp-Ib, and sp-Id are comprised of similar but nonidentical tandemly repeated amino acid sequences. We concluded that sp-Id is encoded by an mRNA whose size and nucleotide sequence organization are similar to Balbiani ring (BR) mRNAs that code for the other sp-I components. Furthermore, parallel repression of sp-Ib and sp-Id synthesis by galactose led us to hypothesize that both of their genes exist within Balbiani ring 2.

Nucleotide sequence of the carboxy-terminal portion of a lodgepole pine actin gene

1988 ◽  
Vol 18 (12) ◽  
pp. 1595-1602 ◽  
Author(s):  
J. R. Kenny ◽  
B. P. Dancik ◽  
L. Z. Florence ◽  
F. E. Nargang
Keyword(s):  
Amino Acid ◽  
Nucleotide Sequence ◽  
Intron Position ◽  
Amino Acid Sequences ◽  
Pairwise Comparisons ◽  
Actin Gene ◽  
Terminal Portion ◽  
The Third ◽  
Actin Genes ◽  
Carboxy Terminal

We have determined the nucleotide sequence of the carboxy-terminal portion of an actin gene (PAc1-A) isolated from Pinuscontorta var. latifolia (Engelm.). Pairwise comparisons of both nucleotide and deduced amino acid sequences were made among PAc1-A, the soybean actins SAc3 and SAc1, maize actin MAc1, chicken β-actin, and yeast β-actin. Of the other actins SAc3 was most similar to the PAc1-A amino acid sequence (91.3% identity) and yeast actin the least similar (78.3% identity). The intron in PAc1-A is present at the same location as the third intron found in MAc1, SAc1, and SAc3 actin genes. This conservation of intron position is unusual when compared with nonplant actin genes.

A head-activator binding protein is present in hydra in a soluble and a membrane-anchored form

Development ◽  
1999 ◽  
Vol 126 (18) ◽  
pp. 4077-4086 ◽  
Author(s):  
W. Hampe ◽  
J. Urny ◽  
I. Franke ◽  
S.A. Hoffmeister-Ullerich ◽  
D. Herrmann ◽  
...  
Keyword(s):  
Stem Cells ◽  
Amino Acid ◽  
Transmembrane Domain ◽  
Binding Protein ◽  
Amino Acid Sequences ◽  
Secreted Protein ◽  
Specific Antibodies ◽  
Head Activator ◽  
Carboxy Terminal

The neuropeptide head activator plays an important role for proliferation and determination of stem cells in hydra. By affinity chromatography a 200 kDa head-activator binding protein, HAB, was isolated from the multiheaded mutant of Chlorohydra viridissima. Partial amino acid sequences were used to clone the HAB cDNA which coded for a receptor with a unique alignment of extracellular modules, a transmembrane domain, and a short carboxy-terminal cytoplasmic tail. A mammalian HAB homologue with identical alignment of these modules is expressed early in brain development. Specific antibodies revealed the presence of HAB in hydra as a transmembrane receptor, but also as secreted protein, both capable of binding head activator. Secretion of HAB during regeneration and expression in regions of high determination potential hint at a role for HAB in regulating the concentration and range of action of head activator.

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