A LOW MOLECULAR WEIGHT ENDOMETRIAL SECRETORY PROTEIN WHICH IS INCREASED BY OVINE TROPHOBLAST PROTEIN-1 IS A β2-MICROGLOBULIN-LIKE PROTEIN

1991 ◽  
Vol 130 (2) ◽  
pp. R1-R4 ◽  
Author(s):  
J. L. Vallet ◽  
P. J. Barker ◽  
G. E. Lamming ◽  
N. Skinner ◽  
N. S. Huskisson
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Secretory Protein ◽  
Explant Culture ◽  
Low Molecular Weight ◽  
Amino Acid Sequencing ◽  
Terminal Amino Acid ◽  
Similar Molecular Weight ◽  
Β2 Microglobulin ◽  
Terminal Amino

ABSTRACT Ovine trophoblast protein-1 (oTP-1), stimulates the secretion of several proteins in explant culture of day-12 cyclic ovine endometrium. We partially purified and identified one of these proteins, an 11,000 Mr, pI approx. 6 protein by N-terminal amino acid sequencing and immunoprecipitation using antibody to human β2-microglobulin. The protein was purified from cultures of endometrium collected from day-16 pregnant ewes. The N-terminal amino acid sequence was 40–55% homologous to β2-microglobulin from a variety of species. Antibody to human β2-microglobulin immunoprecipitated the protein and another protein of similar molecular weight but more acidic pi. Using immunoprecipitation of radiolabelled proteins from culture, we demonstrated that oTP-1 increased production of this protein by 40% (P<0.05). We conclude that oTP-1 increases the secretion of a β2-microglobulin-like protein from day-12 non-pregnant endometrium in culture.

CHARACTERIZATION OF THE PIGMENT OF MICROCOCCUS VIOLAGABRIELLAE

1964 ◽  
Vol 10 (5) ◽  
pp. 659-675 ◽  
Author(s):  
J. N. Campbell ◽  
J. L. Nichols ◽  
Sheila A. Berry
Keyword(s):  
Amino Acids ◽  
Molecular Weight ◽  
Amino Acid ◽  
Cross Reactivity ◽  
Low Molecular Weight ◽  
Terminal Amino Acid ◽  
Iron Chelate ◽  
Peptide Moiety ◽  
Terminal Amino

Production of the red insoluble pigment by Micrococcus violagabriellae was studied. Pigmentation was found to require oxygen and high levels of iron and to be stimulated by tryptophan alone among the amino acids. The pigment was isolated, purified, and analyzed chemically and spectrophotometrically. It was found to be similar to pulcherrimin from Candida pulcherrima. Immunological cross reactivity and analysis of derivatives confirmed the similarity between the bacterial and yeast pigments. From these data it is postulated that the pigment is an iron chelate of pulcherriminic acid with an associated low molecular weight peptide moiety with glycine as the sole N-terminal amino acid. The pigment appears to differ from that of C. pulcherrima solely with respect to this peptide and in the mode of aggregation of the molecule.

High Expression of Human Amelogenin in E. Coli

1996 ◽  
Vol 10 (2) ◽  
pp. 187-194 ◽  
Author(s):  
D. Deutsch ◽  
E. Chityat ◽  
M. Hekmati ◽  
A. Palmon ◽  
Y. Farkash ◽  
...  
Keyword(s):  
Amino Acid ◽  
Western Blotting ◽  
Rt Pcr ◽  
Amino Acid Sequencing ◽  
Terminal Amino Acid ◽  
Expression Plasmid ◽  
Over Expression ◽  
E Coli ◽  
Sds Page ◽  
Terminal Amino

A human cDNA, encoding for the 175-aminoacid human amelogenin, was prepared by RT PCR from tooth bud mRNA and sub-cloned into pGEX-KG expression plasmid for over-expression in E. coli. The expressed protein was characterized by SDS-PAGE, Western blotting, and N-terminal amino acid sequencing.

scholarly journals Purification and Properties of Staphylocoagulase

1975 ◽  
Author(s):  
A.D. Muller ◽  
B. M. Bas ◽  
H. C. Hemker
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Amino Acid Composition ◽  
Aspartic Acid ◽  
Acid Composition ◽  
Isoelectric Point ◽  
Terminal Amino Acid ◽  
Purification And Properties ◽  
Terminal Amino

Staphylocoagulase, an exoprotein of coagulase positive staphylocoagulase, has been purified to a state in which only trace amounts of contaminating proteins are detectable.Purification was more than 35,000 fold, which is 7 times more than the highest value reported in the literature. The yield was about 15%.Aspartic acid was found as a single N-terminal amino acid in this preparation. The molecular weight is 61,000 and the isoelectric point lies at pH 4.53.The amino acid composition was determined.

Physikalische, chemische und biologische Charakterisierung von menschlichem Choriongonadotropin

1968 ◽  
Vol 23 (11) ◽  
pp. 1412-1426 ◽  
Author(s):  
H. D. Schlumberger
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Biological Activities ◽  
Guanidine Hydrochloride ◽  
Group Analysis ◽  
Residual Activity ◽  
Apparent Molecular Weight ◽  
Terminal Amino Acid ◽  
Original Activity ◽  
Terminal Amino

Purification of commercially available HCG preparations with DEAE Sephadex A 50 and Sephadex G 100 column chromatography gave homogeneous fractions having specific biological activities four fold those of the starting materials. The purified HCG has ICSH characteristics and, in high doses, a definite FSH effect is present.Chemical analysis of HCG showed it to contain 29% carbohydrates and 69% peptides. The C-terminal amino acid of the peptide chain was found to be serine, but the N-terminal amino acid could not be determined with normal methods. A molecular weight of 22000 — 27000 daltons was obtained by quantitative end group analysis. Ultracentrifugation experiments in 4 m guanidine hydrochloride gave a molecular weight of 27200 daltons, but in neutral saline solutions at HCG concentrations above 2 mg/ml the apparent molecular weight was higher and indicated dimer formation. A dissociation constant of 10-5 mol/l was estimated for the monomer-dimer equilibrium. Since biological activity is found with 0.1 to 0.5 µg, it was concluded that the HCG monomer is the active entity.The purified HCG is stable from pH 4.5 to pH 10 for 6 hours at 37 °C. At pH 2.5 only 5 to 10% of the original activity is retained. HCG is rapidly inactivated at 100 °C, but a residual activity of 6 — 10% remained after 30 minutes at 80 °C. No activity was lost after 30 minutes incubation at 60 °C.

Isolation and characterization of β-lipolytic hormone from porcine pituitary gland

1970 ◽  
Vol 48 (9) ◽  
pp. 1017-1021 ◽  
Author(s):  
C. Gilardeau ◽  
M. Chrétien
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Pituitary Gland ◽  
Amino Acid Composition ◽  
Biological Activities ◽  
Terminal Amino Acid ◽  
Isolation And Characterization ◽  
Pituitary Glands ◽  
Terminal Amino

A lipolytic substance was isolated from porcine pituitary glands. It's amino acid composition, molecular weight, N-terminal amino acid, isoelectric point, and biological activities are reported. These results are compared to the corresponding values of sheep β-lipolytic hormone.

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