Sequence homology between barley endosperm protein Z and protease inhibitors of the α1‐antitrypsin family

@article{Hejgaard1985SequenceHB,
  title={Sequence homology between barley endosperm protein Z and protease inhibitors of the $\alpha$1‐antitrypsin family},
  author={J{\o}rn Hejgaard and S{\o}ren K. Rasmussen and Anders Brandt and Ib Svendsen},
  journal={FEBS Letters},
  year={1985},
  volume={180},
  url={https://api.semanticscholar.org/CorpusID:84790014}
}
View on Wiley
onlinelibrary.wiley.com
85 Citations
Background Citations
16

85 Citations

A 39 kd barley seed protein of the serpin superfamily inhibits α-chymotrypsin

The 39 kD protein is immunochemically related to the major protein component in beer and reveals a relationship to barley endosperm Z protein which belongs to the serpin superfamily.

Amino‐acid sequence of human α2‐antiplasmin

The amino-acid sequence of human α2-antiplasmin was determined by Edman degradation of peptides purified from CNBr, tryptic and chymotryptic digests by deduced from the cDNA sequence.

A 10 kD barley seed protein homologous with an α-amylase inhibitor from Indian finger millet

A basic protein was isolated from aqueous extracts of barley seeds and NMR-spectroscopy revealed that it possesses tertiary structure and Amino acid composition and N-terminal sequence show that it corresponds to the probable amylase/protease inhibitor (PAPI) encoded by a formerly described cDNA.

A recombinant wheat serpin with inhibitory activity

Southern blots and amino acid sequencing indicated that only few serpins are encoded by wheat, but at least three distinct genes are expressed in the grain, including WSZ1, which belongs to the subfamily of protein Z-type serpins.

A plant serpin gene. Structure, organization and expression of the gene encoding barley protein Z4.

The deduced amino acid sequence, which was corroborated by peptide sequences, consists of 399 amino acids and has a molecular mass of 43,128 Da, which confirms protein Z4 to be a member of the serpin superfamily of proteins.

Serpins from wheat grain

Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization.

Comparison of the amino acid and cDNA sequences indicates that secretion is mediated by a 22-residue signal peptide and that further proteolytic processing does not occur; C1 inhibitor is a member of the large serine protease inhibitor (serpin) gene family.

Complete amino acid sequence of the α-amylase/subtilisin inhibitor from barley

The complete amino acid sequence of the α-amylase/subtilisin inhibitor (BASI) isolated from barley has been determined by Edman degradation using spinning cup as well as gas-phase sequencing.…

Inhibitory Serpins from Wheat Grain with Reactive Centers Resembling Glutamine-rich Repeats of Prolamin Storage Proteins

Five serpins identified in grains of hexaploid bread wheat were suicide substrate inhibitors of chymotrypsin and cathepsin G and possible functions involving interactions with endogenous or exogenous proteinases adapted to prolamin degradation are discussed.

COMPLETE AMINO ACID SEQUENCE OF THE (~-AMYLASE/SUBTILISlN INHIBITOR FROM BARLEY

    Biology, Chemistry
  • 2008
The complete amino acid sequence of the ct-amylase/subtilisin inhibitor (BASI) isolated from barley has been determined by Edman degradation using spinning cup as well as gas-phase sequencing.…
...

21 References

A cDNA clone for protein Z, a major barley endosperm albumin

In vitro translation of barley endosperm mRNA and subsequent immunoaffinity isolation using protein Z antibodies identified two major protein Z precursor polypeptides of M.W.44,000 among the translation products.

Characteristics of Hiproly barley III. Amino acid sequences of two lysine-rich proteins

Two lysine-rich components isolated from «Hiproly» barley have been subjected to sequence determination. The complete sequence of the smallest component, designated SP II B, has been determined. This…

Cloning and sequence of cDNA coding for alpha 1-antitrypsin.

Comparison of the amino acid sequences of baboon alpha 1-antitrypsin, human antithrombin III, and chicken ovalbumin indicated that these three proteins are about 230% homologous.

Purification and properties of protein Z – a major albumin of barley endosperm

A major albumin of barley grain, called protein Z, has been purified from endosperm flour and resulted in a highly pure protein as judged from various electrophoretic and immunoelectrophoretics tests.

Sequence homology between human alpha 1-antichymotrypsin, alpha 1-antitrypsin, and antithrombin III.

Comparison of the amino acid sequence of alpha 1-antichymotrypsin with that of the human alpha1-antitrypsIn has revealed a homology level similar to that between chymotRYpsin and trypsin.

Plasma protease inhibitors in mouse and man: divergence within the reactive centre regions

It is proposed that the genes for contrapsin and human α1-antichymotrypsin are the dependents of a single gene that have evolved since rodent and primate divergence to encode proteins with different functions.

The amino acid sequence of the large plakalbumin peptide and the C-terminal sequence of ovalbumin.

The amino acid sequence of a 33-residue peptide isolated from plakalbumin by gel filtration in 6M urea at pH 3 and derived from the C-terminal portion of ovalbumin has been determined. Enzyme…

Organization and transcription of B1 hordein genes in high lysine mutants of barley

Failure of these RNA sequences to be translated into B1 hordein polypeptides in a cell free protein synthesizing system hints that thelys3a gene is involved in the post-transcriptional modification of the messenger RNA.

Free and Protein-bound β-Amylases of Barley Grain. Characterization by Two-dimensional Immunoelectrophoresis

The aggregated form of β-amylase was found to predominate in extracts made in the presence of papain, and possible functions of the non-enzymatic protein in formation of latent β- amylase is discussed.

Primary structure of human preangiotensinogen deduced from the cloned cDNA sequence.

Analyses by nucleotide sequence determination, S1 nuclease mapping, and RNA blot hybridization indicate that human preangiotensinogen is encoded by two mRNAs that differ only in the length of the 3'-untranslated region.