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B Wittmann-Liebold

Publications and source records attributed to B Wittmann-Liebold.

At least 127 records · Page 7Linked to original sources
PubMed1980

The primary structure of histone H1 from sperm of the sea urchin Parechinus angulosus. 1. Chemical and enzymatic fragmentation of the protein and the sequence of amino acids in the four N-terminal cyanogen bromide peptides.

The primary structure of the amino-terminal 84 residues of sperm histone H1Parechinus has been determined. The sequence is: Pro-Gly-Ser-Pro-Gln-Lys-Arg-Ala-Ala-Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys-Ser-Pro-Lys-Lys-Ser-Pro-Arg-Lys-Ala-Ser-Ala-Ser-Pro-Arg-Arg-Lys-Ala-Lys-Arg-Ala-Arg-Ala-Ser-Thr-His-Pro-Pro-Val-Leu-Glu-Met-Val-Gln-Ala-Ala-Ile-Thr-Ala-Met-Lys-Glu-Arg-Lys-Gly-Ser-Ser-Ala-Ala-Lys-Ile-Lys-Ser-Tyr-Met-Ala-Ala-Asn-Tyr-Arg-Val-Asp-Met-Asn-Val-Leu-Ala-Pro-.

Amino Acid Sequence↗
PubMed1980

The primary structure of histone H1 from sperm of the sea urchin Parechinus angulosus. 2. Sequence of the C-terminal CNBr peptide and the entire primary structure.

The primary structure of sperm histone H1Parechinus has been determined. H1Parechinus consists of a polypeptide chain of the following 248 amino acid residues: Pro-Gly-Ser-Pro-Gln-Lys-Arg-Ala-Ala-Ser-Pro-Arg-Lys-Ser-Pro-Arg-Lys-Ser-Pro-Lys-Lys-Ser-Pro-Arg-Lys-Ala-Ser-Ala-Ser-Pro-Arg-Arg-Lys-Ala-Lys-Arg-Ala-Arg-Ala-Ser-Thr-His-Pro-Pro-Val-Leu-Glu-Met-Val-Gln-Ala-Ala-Ile-Thr-Ala-Met-Lys-Glu-Arg-Lys-Gly-Ser-Ser-Ala-Ala-Lys-Ile-Lys-Ser-Tyr-Met-Ala-Ala-Asn-Tyr-Arg-Val-Asp-Met-Asn-Val-Leu-Ala-Pro-His-Val-Arg-Arg-Ala-Leu-Arg-Asn-Gly-Val-Ala-Ser-Gly-Ala-Leu-Lys-Gln-Val-Thr-Gly-Thr-Gly-Ala-Ser-Gly-Arg-Phe-Arg-Val-Gly-Ala-Val-Ala-Lys-Pro-Lys-Lys-Ala-Lys-Lys-Thr-Ser-Ala-Ala-Ala-Lys-Ala-Lys-Lys-Ala-Lys-Ala-Ala-Ala-Ala-Lys-Lys-Ala-Arg-Arg-leads to Lys-Ala-Lys-Ala-Ala-Ala-Lys-Arg-Lys-Ala-Ala-Leu-Ala-Lys-Lys-Lys-Ala-Ala-Ala-Ala-Lys-Arg-Lys-Ala-Ala-Ala-Lys-Ala-Lys-Lys-Ala-Lys-Lys-Pro-Lys-Lys-Lys-Ala-Ala-Ala-Lys-Lys-Ala-Lys-Lys-Pro-Ala-Lys-Lys-Ser-Pro-Lys-Lys-Ala-Lys-Lys-Pro-Ala-Lys-Lys-Ser-Pro-Lys-Lys-Lys-Lys-Ala-Lys-Arg-Ser-Pro-Lys-Lys-Ala-Lys-Lys-Ala-Ala-Gly-Lys-Arg-Lys-Pro-Ala-Ala-Lys-Lys-Ala-Arg-Arg-Ser-Pro-Arg-Lys-Ala-Gly-Lys-Arg-Arg-Ser-Pro-Lys-Lys-Ala-Arg-Lys. The protein consists of three domains. Compared to other H1 and H5 histones, there is a very similar hydrophobic central domain and the carboxyl-terminal domain is very rich in lysine and alanine. H1Parechinus is similar to H5 histones in that the carboxyl-terminal domain also contains many arginine residues close to the carboxyl terminus. The carboxyl-terminal domain of H1Parechinus appears to have been constructed by a series of variable duplications. The amino-terminal domain of H1Parechinus is longer and quire different to that of other H1 and H5 histones and is characterized by a repeating tetrapeptide of the general type Ser-Pro-(basic)2. The known sequence of a histone H1 gene from Psammechinus miliaris [Schaffner, W. et al. (1978) Cell, 14, 655-671] is compared to the sequence of H1Parechinus. Again the central hydrophobic domains are similar whereas the amino terminal domains are very different. The functions of the various domains of sperm histone H1Parechinus are discussed.

Amino Acid Sequence↗
PubMed1980

Purification and primary structure determination of the N-terminal blocked protein, L11, from Escherichia coli ribosomes.

Protein L11 was isolated from the 50-S subunit of Escherichia coli ribosomes, using two salt extractions and two chromatographic separations on CM-cellulose. The unusual behavior of the protein when run on sodium dodecyl sulfate electrophoresis showed multiple bands. The complete primary structure of protein L11 is presented in detail. Its sequence was derived from peptides obtained by digesting the protein with trypsin, chymotrypsin, thermolysin, Staphylococcus aureus protease and, after modification, with trypsin. Chemical cleavage was performed with cyanogen bromide. Sequencing of the various peptides was achieved by manual micro-dansyl-Edman degradations and automatic methods. The N-terminal residue of the protein is blocked and was not degradable in the liquid-phase sequenator by the Edman method. It was identified by a combination of enzymatic cleavage and mass spectrometry. Protein L11 contain three methylated amino acid residues, a N alpha-trimethylalanine, and two residues of N epsilon-trimethyllysine. Their behaviour and influence in the sequence elucidation are described. The protein contains 141 amino acid residues and has a molecular weight of 14874. Secondary structure predictions of the protein are given, and its sequence is compared with those of other E. coli ribosomal proteins.

Amino Acid Sequence↗
PubMed1980

Identification of methylated amino acids during sequence analysis. Application to the Escherichia coli ribosomal protein L11.

Three methylated amino acid residues, one residue of N-trimethylalanine and two of N epsilon,N epsilon,N epsilon-trimethyllysine residues, are present in protein L11. The methods used for the identification and location of these unusual amino acids in the sequence of protein L11 are described. Temperature and pH modifications to the eluting buffers enabled the detection of the methylated derivatives of lysine and arginine with a Durrum analyser using routine 90 min amino acid analyses. The presence of N epsilon,N epsilon-dimethyllysine in the hydrolysate of proteins, was revealed by ascending chromatography on thin-layer cellulose plates. The blocked N-terminal amino acid of protein L11, N,N,N-trimethylalanine, although non-volatile, was identified by field desorption mass spectrometry. The identification was confirmed by comparing the N-terminal dipeptide of protein L11 with the synthesised dipeptide Me3Ala-Lys. The behaviour of these methylated amino acids during sequence analysis is described.

Alanine↗
PubMed1980

The primary structure of Bacillus subtilis acidic ribonsomal protein B-19. Isolation and characterization of peptides and the complete amino acid sequence.

The complete primary structure of Bacillus subtilis acidic protein B-L9, functionally equivalent to protein L7/L12 from E. coli, has been determined. B-L9 is composed of 122 residues and has the amino acid composition: Asp3, ASN3, Thr4, Ser3, Glu22, Gln1, Pro3, Gly11, Ala21, Val14, Ile9, Leu12, Phe2, Lys13, and Arg1. The molecular weight of B-L9 is 12,633. The amino acid sequence was determined by a combination of automated Edman degradation of the intact protein in a modified Beckman sequenator, and micro dansyl-Edman degradation of the peptides obtained from digestions with trypsin, thermolysin, Staphylococcus aureus protease, chymotrypsin and pepsin. A comparison of protein B-L9 from B. subtilis with E-L12 from E. coli shows a relatively high degree of homology.

Amino Acid Sequence↗
PubMed1979

Amino acid sequence of the ribosomal protein L21 of Escherichia coli.

The primary structure of protein L21 from the 50S subunit of Escherichia coli ribosomes has been completely determined by sequencing the peptides obtained by digestion of L21 with trypsin before and after modification of the arginine residues with 1,2-cyclohexanedione, Staphylococcus aureus protease, thermolysin, and pepsin. Automated Edman degradation using a liquid-phase sequenator was carried out on the intact protein as well as on a fragment arising from cleavage with cyanogen bromide. Protein L21 consists of a single polypeptide chain of 103 amino acids of molecular weight 11 565. An estimation of the secondary structure of protein L21 and a comparison with other E. coli ribosomal protein sequences are presented.

Amino Acid Sequence↗
PubMed1979

Sequence of the amino-terminal region of rat liver ribosomal proteins S4, S6, S8, L6, L7a, L18, L27, L30, L37, L37a, and L39.

The sequence of the amino-terminal region of eleven rat liver ribosomal proteins--S4, S6, S8, L6, L7a, L18, L27, L30, L37a, and L39--was determined. The analysis confirmed the homogeneity of the proteins and suggests that they are unique, since no extensive common sequences were found. The N-terminal regions of the rat liver proteins were compared with amino acid sequences in Saccharomyces cerevisiae and in Escherichia coli ribosomal proteins. It seems likely that the proteins L37 from rat liver and Y55 from yeast ribosomes are homologous. It is possible that rat liver L7a or L37a or both are related to S cerevisiae Y44, although the similar sequences are at the amino-terminus of the rat liver proteins and in an internal region of Y44. A number of similarities in the sequences of rat liver and E coli ribosomal proteins have been found; however, it is not yet possible to say whether they connote a common ancestry.

Amino Acid Sequence↗
PubMed1979

The primary structure of ribosomal protein S7 from E. coli strains K and B.

Ribosomal proteins S7 from 30S subunits of Escherichia coli strains K and B differ extensively in their aminoacid compositions. The experimental details which led to the determination of the complete primary structures of proteins S7K and S7B are presented. Protein S7K consists of a single polypeptide chain of 177 aminoacids giving a calculated molecular weight of 19, 732, whereas protein S7B has 153 residues which amount to a molecular weight of 17,131. Aminoacid sequences were determined by a combination of automated Edman degradation of the intact proteins in a modified Beckman sequenator and sequencing of peptides obtained by digestion with trypsin. Staphylococcus aureus protease, thermolysin and pepsin, either by solid-phase Edman degradation or by dansyl-Edman degradation. Additional information about the primary structure was derived from peptides resulting from chemical cleavages of the protein by 2-(2-nitrophenyl-sulphenyl)-3-methyl 3' bromoindolenine at its tryptophanyl bonds and by cyanogen bromide at its methionyl bonds leading to large fragments. The mutational event occurring between S7B and S7K was characterized. Protein S7K contains an additional sequence of 24 aminoacids at its C-terminal end. The aminoacid sequence of both proteins S7K and S7B was compared to the published sequences of the other ribosomal proteins of Escherichia coli and predictions for the secondary structure of these proteins were made.

Amino Acid Sequence↗
PubMed1978

The complete amino-acid sequence of histone H2B(3) from sperm of the sea urchin Parechinus angulosus.

The primary structure of a third H2B histone isolated from sperm of the sea urchin Parechinus angulosus has been determined. H2B(3) consists of a polypeptide chain of the following 148 amino acid residues: Pro-Arg-Ser-Pro-Ala-Lys-Thr-Ser-Pro-Arg-Lys-Gly-Ser-Pro-Arg-Lys-Gly-Ser-Pro-Arg-Lys-Gly-Ser-Pro-Ser-Arg-Lys-Ala-Ser-Pro-Lys-Arg-Gly-Gly-Lys-Gly-Ala-Lys-Arg-Ala-Gly-Lys-Gly-Gly-Arg-Arg-Arg-Arg-Val-Val-Lys-Arg-Arg-Arg-Arg-Arg-Arg-Glu-Ser-Tyr-Gly-Ile-Tyr-Ile-Tyr-Lys-Val-Leu-Lys-Gln-Val-His-Pro-Asp-Thr-Gly-Ile-Ser-Ser-Arg-Ala-Met-Ser-Val-Met-Asn-Ser-Phe-Val-Asn-Asp-Val-Phe-Glu-Arg-Ile-Ala-Ser-Glu-Ala-Ser-Arg-Leu-Thr-Ser-Ala-Asn-Arg-Arg-Ser-Thr-Val-Ser-Ser-Arg-Glu-Ile-gln-Thr-Ala-Val-Arg-Leu-Leu-Leu-Pro-Gly-Glu-Leu-Ala-Lys-His-Ala-Val-Ser-Glu-Gly-Thr-Lys-Ala-Val-Thr-Lys-Tyr-Thr-Thr-Ser-Arg. H2B(3) Parechinus closely resembles HIB(2) Parechinus but has one additional repeating pentapeptide in the amino-terminal region and a serine replacing glycine at position 98.

Amino Acid Sequence↗