scholarly journals Complete amino acid sequence of BSP-A3 from bovine seminal plasma. Homology to PDC-109 and to the collagen-binding domain of fibronectin

1987 ◽  
Vol 243 (1) ◽  
pp. 195-203 ◽  
Author(s):  
N G Seidah ◽  
P Manjunath ◽  
J Rochemont ◽  
M R Sairam ◽  
M Chrétien
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Complete Characterization ◽  
Binding Domain ◽  
Collagen Binding ◽  
Ancestral Gene ◽  
Complete Amino Acid Sequence ◽  
Molecular Variants

Bovine seminal plasma was shown to contain three similar proteins, called BSP-A1, BSP-A2 and BSP-A3. Both BSP-A1 and BSP-A2 were shown to be molecular variants of a recently characterized peptide called PDC-109. They seem to differ only in their degree of glycosylation and otherwise seem to possess an identical amino acid composition. The work in the present paper deals with the complete characterization of the third member of this series, namely BSP-A3. The complete amino acid sequence revealed that it is composed of 115 amino acids and predicts a Mr of 13,403. An analysis of the primary structure of BSP-A3 revealed a high degree of internal homology, with two homologous domains composed of 39 (residues 28-66) and 43 (residues 73-115) amino acids. An exhaustive computer-bank search for the similarity of this sequence to any known protein, or segment thereof, revealed two significant homologies. The first is between PDC-109 and BSP-A3, which is so high that we can confidently predict that both proteins evolved from a single ancestral gene. The collagen-binding domain of bovine fibronectin (type II sequence) was also found to be highly homologous to both BSP-A3 and PDC-109.

scholarly journals Amino acid sequence of HSP-1, a major protein of stallion seminal plasma: effect of glycosylation on its heparin- and gelatin-binding capabilities

1995 ◽  
Vol 310 (2) ◽  
pp. 615-622 ◽  
Author(s):  
J J Calvete ◽  
K Mann ◽  
W Schäfer ◽  
L Sanz ◽  
M Reinert ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Binding Activity ◽  
Size Exclusion ◽  
Major Protein ◽  
Heparin Binding ◽  
Aggregation State ◽  
Consensus Pattern

We report the complete amino acid sequence of HSP-1, a major protein isolated from stallion seminal plasma or acid extracts of ejaculated spermatozoa. The protein consists of 121 amino acids organized in two types of homologous repeats arranged in the pattern AA‘BB’. Each of the 13-15-residue A-type repeats contains two O-linked oligosaccharide chains. The B-type repeats span 44-47 amino acids each, are not glycosylated, and have the consensus pattern of the gelatin-binding fibronectin type-II module. This domain also occurs in the major bovine seminal plasma heparin-binding proteins PDC-109 (BSP-A1/A2) and BSP-A3. However, unlike the bovine proteins which bind quantitatively to a heparin-Sepharose column, stallion HSP-1 was recovered in both the flow-through and the heparin-bound fractions. Structural analysis showed that the two HSP-1 forms contain identical polypeptide chains which are differently glycosylated. Moreover, size-exclusion chromatography showed that heparin-bound HSP-1 associates with HSP-2, another major seminal plasma protein, into a 90 kDa product, whereas the non-heparin-bound glycoform of HSP-1 is eluted as a monomeric (14 kDa) protein. This suggests that glycosylation may have an indirect effect on the heparin-binding ability of HSP-1 through modulation of its aggregation state. On the other hand, both glycoforms of HSP-1 displayed gelatin-binding activity, indicating that the molecular determinants for binding heparin and gelatin are different.

scholarly journals The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain.

1989 ◽  
Vol 109 (1) ◽  
pp. 397-407 ◽  
Author(s):  
Y Takada ◽  
M E Hemler
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Matrix Protein ◽  
Transmembrane Domain ◽  
Cdna Clones ◽  
Terminal Sequence ◽  
Collagen Binding ◽  
Collagen Receptor ◽  
Integrin Family

VLA-2 (also called gpIa/IIa on platelets) is a collagen receptor with a unique alpha subunit and a beta subunit common to other adhesion receptors in the VLA/integrin family. Multiple cDNA clones for the human VLA-2 alpha 2 subunit have been selected from a lambda gtll library by specific antibody screening. The 5,374-bp nucleotide sequence encoded for 1,181 amino acids, including a signal peptide of 29 amino acids followed by a long extracellular domain (1,103 amino acids), a transmembrane domain, and a short cytoplasmic segment (22 amino acids). Direct sequencing of purified alpha 2 protein confirmed the identity of the 15 NH2-terminal amino acids. Overall, the alpha 2 amino acid sequence was 18-25% similar to the sequences known for other integrin alpha subunits. In particular, the alpha 2 sequence matched other integrin alpha chains in (a) the positions of 17 of its 20 cysteine residues; (b) the presence of three metal-binding domains of the general structure DXDXDGXXD; and (c) the transmembrane domain sequence. In addition, the alpha 2 sequence has a 191-amino acid insert (called the I-domain), previously found only in leukocyte integrins of the beta 2 integrin family. The alpha 2 I-domain was 23-41% similar to domains in cartilage matrix protein and von Willebrand factor, which are perhaps associated with collagen binding. The NH2-terminal sequence reported here for alpha 2 does not match the previously reported alpha 2 NH2-terminal sequence (Takada, Y., J. L. Strominger, and M. E. Hemler. 1987. Proc. Natl. Acad. Sci. USA. 84:3239-3243). Resolution of this discrepancy suggests that there may be another VLA heterodimer that resembles VLA-2 in size but has a different amino acid sequence.

The structure and function of the epidermal growth factor receptor studied by using antisynthetic peptide antibodies

1985 ◽  
Vol 226 (1242) ◽  
pp. 127-134 ◽  
Keyword(s):  
Amino Acids ◽  
Epidermal Growth Factor Receptor ◽  
Amino Acid ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Amino Acid Sequence ◽  
Egf Receptor ◽  
Growth Factor Receptor ◽  
Binding Domain ◽  
Epidermal Growth

The human epidermal growth factor receptor has been purified and partial amino acid sequence obtained. A synthetic oligonucleotide was used to select complementary DNA clones from placental and A431 clone banks. The nucleotide sequence of a 5.8 kilobase transcript was determined and used to predict the total amino acid sequence of the receptor. We have predicted a model for the receptor which has an external ligand binding domain of 621 amino acids, a transmembrane region of 23 amino acids, and a cytoplasmic domain of 542 amino acids having protein tyrosine kinase activity. The kinase autophosphorylation sites have been mapped onto the primary amino acid sequence. Analysis of protein sequence databases have shown that the erb -B oncogene of avian erythroblastosis virus has acquired part of the avian EGF receptor gene. The hypothesis has been proposed that transformation by this virus is the result of expression of a truncated EGF receptor which lacks the majority of the EGF binding domain and delivers a continuous proliferation signal to transformed cells. We describe here the production of polyclonal and monoclonal antibodies to selected synthetic peptides from the EGF receptor and v-erb B sequences. Antisera to sequences encompassing the three major sites of autophosphorylation and the putative ATP binding site all recognize the native EGF receptor molecule. We have used these reagents to test our model of EGF receptor structure and v-erb B function.

Complete Amino-Acid Sequence of Bovine Seminal Ribonuclease, a Dimeric Protein from Seminal Plasma

1987 ◽  
Vol 368 (2) ◽  
pp. 1305-1312 ◽  
Author(s):  
Hisanori SUZUKI ◽  
Augusto PARENTE ◽  
Benedetta FARINA ◽  
Luigi GRECO ◽  
Renato LA MONTAGNA ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Ribonuclease A ◽  
Complete Amino Acid Sequence ◽  
Bovine Seminal Ribonuclease ◽  
Dimeric Protein

Molecular cloning of cDNA for porcine prolactin precursor

1990 ◽  
Vol 4 (2) ◽  
pp. 135-142 ◽  
Author(s):  
Y. Kato ◽  
T. Hirai ◽  
T. Kato
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Signal Sequence ◽  
Cdna Clones ◽  
Amino Acid Residues ◽  
Ancestral Gene ◽  
Wide Range ◽  
Hydrophilic Residues ◽  
Ovine Prolactin

ABSTRACT Porcine prolactin cDNA clones were screened using antiserum against ovine prolactin from a cDNA library of porcine anterior pituitary, and their nucleotide sequences were determined by the chain-termination method. The nucleotide sequence of the 5′ untranslated region and part of the signal peptide region were determined by direct RNA sequencing with reverse transcriptase. The composite sequence of 957 nucleotides showed a signal sequence of 30 amino acids and a further 199 amino acids corresponding to the mature prolactin molecule. The predicted sequence confirmed the amino acid sequence determined previously by direct protein analysis, except for one amide form at residue 122 (Gln instead of the reported Glu). Northern blot analysis showed that the length of the porcine prolactin mRNA was about 1·1 kb. The porcine prolactin amino acid sequence showed 81, 80, 64, 62, 80 and 31% homology with human, bovine, rat, mouse, chick and salmon forms respectively. The identical amino acid residues showed marked clustering in four domains, two of which are highly conserved throughout a wide range of species. The hydropathy and secondary structure of porcine prolactin were analysed and compared with those of porcine GH, which shares the same ancestral gene. The two highly conserved regions of both hormones showed similar hydrophilicity, and the predicted secondary structures indicated that these regions in each hormone form different structures with differences in extension of the hydrophilic residues outside the molecule.

scholarly journals Complete amino acid sequence of Shigella toxin B-chain. A novel polypeptide containing 69 amino acids and one disulfide bridge.

1986 ◽  
Vol 261 (30) ◽  
pp. 13928-13931
Author(s):  
N G Seidah ◽  
A Donohue-Rolfe ◽  
C Lazure ◽  
F Auclair ◽  
G T Keusch ◽  
...  
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Disulfide Bridge ◽  
Toxin B ◽  
Complete Amino Acid Sequence

Complete amino acid sequence of human seminal plasma β-inhibin

FEBS Letters ◽  
1984 ◽  
Vol 175 (2) ◽  
pp. 349-355 ◽  
Author(s):  
N.G. Seidah ◽  
N.J. Arbatti ◽  
J. Rochemont ◽  
A.R. Sheth ◽  
M. Chrétien
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Seminal Plasma ◽  
Human Seminal Plasma ◽  
Complete Amino Acid Sequence

scholarly journals The primary structure of a short neurotoxin homologue from Dendroaspis polylepis polylepis (Black mamba) venom

1984 ◽  
Vol 3 (3) ◽  
pp. 169-174
Author(s):  
F. J. Joubert
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Sequence ◽  
Primary Structure ◽  
Gel Filtration ◽  
Cysteine Residues ◽  
Complete Amino Acid Sequence

Toxin CM-7 was purified from black mamba venom by gel filtration on Sephadex G-50 followed by ion exchange chromotography on CM-cellulose. It contains 60 amino acids, including eight half-cystines. The complete amino acid sequence of toxin CM-7 has been elucidated. In toxin CM-7 the eleven structurally invariant amino acids of the neurotoxins and cardiotoxins are conserved, but it has only one of the five functionally invariant amino acids of the neurotoxins. The eight cysteine residues of toxin CM-7 are in the same locations as those in short neurotoxins of known structures and are presumed to be similarly cross-linked. The sequence of CM-7 is structurally homologous with the short neurotoxins, but it is less toxic.

A Gastric Inhibitory Polypeptide II: The Complete Amino Acid Sequence

1971 ◽  
Vol 49 (8) ◽  
pp. 867-872 ◽  
Author(s):  
John C. Brown ◽  
Jill R. Dryburgh
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Amino Acid Residue ◽  
Gastric Inhibitory Polypeptide ◽  
Complete Amino Acid Sequence ◽  
Calculated Molecular Weight ◽  
Residue Polypeptide

Porcine gastric inhibitory polypeptide is a 43 amino acid residue polypeptide with the amino acid sequence Tyr–Ala–Glu–Gly–Thr–Phe–Ile–Ser–Asp–Tyr–Ser–Ile–Ala–Met–Asp–Lys–Ile–Arg–Gln–Gln–Asp–Phe–Val–Asn–Trp–Leu–Leu–Ala–Gln–Gln–Lys–Gly–Lys–Lys–Ser–Asp–Trp–Lys–His–Asn–Ile–Thr–Gln. Fifteen of the first 26 amino acids occur in the same position as they do in porcine glucagon, and nine of the first 26 in the same position as in porcine secretin. The calculated molecular weight of the polypeptide is 5105.

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