scholarly journals Studies on the Nature of Prolactin-Like Immunoreactivity in Bromelin-Treated Cervical Mucus

1985 ◽  
Vol 22 (3) ◽  
pp. 316-320
Author(s):  
Han-Zheng Wang ◽  
A Donaldson ◽  
SB Sufi ◽  
SL Jeffcoate
Keyword(s):  
Molecular Weight ◽  
Cervical Mucus ◽  
Similar Molecular Weight ◽  
Biological Matrix ◽  
Pituitary Prolactin

Prolactin has been reported to be present in cervical mucus at concentrations higher than those found in blood. Our initial findings appeared to confirm this and the material fulfilled criteria of validity generally applied when an immunoassay is employed on a new biological matrix, i.e. parallelism and chromatographic identity. Further experiments demonstrated that prolactin concentrations in cervical mucus were less than 40 mU/L and the prolactin-like immunoreactivity originally detected was due to the action of the enzyme bromelin which was used to liquefy the mucus. Bromelin has a similar molecular weight to prolactin and appeared to digest prolactin tracer and reduce its ability to bind antiserum in a manner paralleling the effect of adding pituitary prolactin.

scholarly journals Immunohistochemical and immunochemical characterization of a new endothelial cell-specific antigen.

1986 ◽  
Vol 34 (2) ◽  
pp. 209-214 ◽  
Author(s):  
J U Alles ◽  
K Bosslet
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
Endothelial Cells ◽  
Endothelial Cell ◽  
Specific Antigen ◽  
Similar Molecular Weight ◽  
Immunochemical Characterization ◽  
Sds Page

A new monoclonal antibody (moab BW 200) of IgG3 kappa-isotype was generated which recognizes an epitope located on an antigen molecule restricted to human neoplastic and non-neoplastic endothelial cells. The molecular weight of the antigen was determined using immunoprecipitation analysis followed by SDS-PAGE. Despite its similar molecular weight to FVIII-RAG, the antigen detected by moab BW 200 was shown to be different from FVIII-RAG.

scholarly journals The composition of peptidochitodextrins from sarcophagid puparial cases

1971 ◽  
Vol 125 (3) ◽  
pp. 703-716 ◽  
Author(s):  
H. Lipke ◽  
T. Geoghegan
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Protein Complex ◽  
Covalent Bonds ◽  
Aromatic Residues ◽  
Similar Molecular Weight ◽  
X Ray ◽  
Molecular Weights ◽  
Physical Interactions ◽  
The Stability

1. N-Bromosuccinimide cleaved proteins and pigments from fly puparia, increasing the chitin:protein ratio from 0.5 to 1.5. The product afforded subfractions (ratio 5:1) of molecular weights of 1200 and 1600 devoid of aromatic residues and N-terminal β-alanine, direct aryl links between polysaccharide chains being discounted. 2. The chitin–protein complex decreased in molecular weight when treated with Pronase, which suggested polypeptide bridges within the native chitin micelle. The limit dextrins generated by chitinase were mixtures of unsubstituted dextrins and peptidylated oligosaccharides, with the former predominating. 3. Peptidochitodextrins of similar molecular weight but markedly different solubility were prepared, which were indistinguishable with respect to amino acid, glucosamine, acetyl, X-ray or infrared characteristics. It is suggested that physical interactions contribute to the stability of the integument in addition to the covalent bonds that form during sclerotization.

scholarly journals Protein diffusion through charged nanopores with different radii at low ionic strength

2014 ◽  
Vol 16 (39) ◽  
pp. 21570-21576 ◽  
Author(s):  
Pieter Stroeve ◽  
Masoud Rahman ◽  
Lekkala Dev Naidu ◽  
Gilbert Chu ◽  
Morteza Mahmoudi ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Ionic Strength ◽  
Protein Diffusion ◽  
Similar Molecular Weight ◽  
Low Ionic Strength ◽  
Charged Membranes ◽  
Pore Permeability

Pore permeability for two similar molecular weight proteins (BSA and BHb) through nanoporous charged membranes at low ionic strength (I = 0.001 M).

scholarly journals Trypsin inhibitors in turnip (Brassica rapa L.) seeds

2014 ◽  
Vol 58 (4) ◽  
pp. 563-573 ◽  
Author(s):  
Anna Wilimowska-Pelc
Keyword(s):  
Molecular Weight ◽  
Peptide Bond ◽  
Ion Exchange Chromatography ◽  
Trypsin Inhibitors ◽  
Exchange Chromatography ◽  
Trypsin Activity ◽  
Reactive Site ◽  
Salting Out ◽  
Similar Molecular Weight ◽  
Immobilized Trypsin

A method of trypsin inhibitors isolation from turnip seeds is described. Inhibitors were extracted with 0.01 N HCI, concentrated by salting out with ammonium sulfate, and purified using ion-exchange chromatography on Sp-Sephadex C-25, QAE-Sephadex A-25 and affinity chromatography on immobilized trypsin. Among the three isolated inhibitors, ITR I of molecular weight 15.9 kDa, pl. 6,4, inhibited trypsin activity only. Inhibitors ITR II and ITR Ill inhibited also chymotrypsin activity, they had similar molecular weight (about 10 kDa), but their pI is 7.5 and over 10, respectively. Arginine residue occurred in P, position of the reactive site of inhibitors ITR I and ITR III, while in ITR 11 this position was occupied by lysine residue. Electrophoresis on polyacrylamide gel revealed that each inhibitor possessed two protein fractions, probably a virgin and modified form, with the reactive site peptide bond broken by trypsin.

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.

scholarly journals Isolation of the JMH antigen on a novel phosphatidylinositol-linked human membrane protein

Blood ◽  
1992 ◽  
Vol 79 (6) ◽  
pp. 1574-1581 ◽  
Author(s):  
KA Bobolis ◽  
JJ Moulds ◽  
MJ Telen
Keyword(s):  
Molecular Weight ◽  
Monoclonal Antibody ◽  
T Cell ◽  
Membrane Protein ◽  
Cell Line ◽  
Human Erythrocyte ◽  
High Frequency ◽  
Paroxysmal Nocturnal Hemoglobinuria ◽  
Blood Group Antigen ◽  
Similar Molecular Weight

Abstract JMH is a high-frequency human erythrocyte blood group antigen. Previous work has shown that JMH is absent from complement-sensitive erythrocytes of patients with paroxysmal nocturnal hemoglobinuria (PNH); such cells have a broad defect in expression of phosphatidylinositol (PI)-linked proteins. Using both human JMH antisera and a JMH-like murine monoclonal antibody, we have identified a 76-Kd membrane protein present in JMH-positive but not JMH-negative erythrocytes. A similar 76-Kd JMH protein was also identified on a human lymphoid T-cell line, HSB-2. Using PI-specific phospholipase C, a small amount of JMH antigen could be cleaved from intact erythrocytes and immunoprecipitated from the supernate of treated erythrocytes, thus confirming that the protein bearing the JMH antigen is anchored by a PI- linkage to the erythrocyte membrane. This protein was further shown not to be identical to decay accelerating factor (70 Kd), a previously identified PI-anchored protein of somewhat similar molecular weight.

A MvaI PCR-RFLP detecting a silent allele at the goat α-lactalbumin locus

2003 ◽  
Vol 70 (3) ◽  
pp. 355-357 ◽  
Author(s):  
Gianfranco Cosenza ◽  
Daniela Gallo ◽  
Rosa Illario ◽  
Paola di Gregorio ◽  
Carmela Senese ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Common Ancestor ◽  
Polypeptide Chain ◽  
Serum Proteins ◽  
Transcription Unit ◽  
Human Lysozyme ◽  
Similar Molecular Weight ◽  
Pcr Rflp ◽  
Lactose Synthase ◽  
Silent Allele

Alpha-lactalbumin (α-la), a calcium metalloprotein, is one of the major serum-proteins in ruminant milk (Jenness, 1982) and induces lactose synthesis in the mammary gland by interacting with the enzyme UDP-galactosyltransferase, giving rise to the heterodimer enzyme lactose synthase (Ebner & Brodbeck, 1968; Kuhn, 1983). The goat α-la transcription unit (LALBA), located on chromosome 5 (Hayes et al. 1993), is organized in 4 exons varying in length from 75 nucleotides (3rd exon) to 329 nucleotides (4th exon) coding for a 123-amino acid polypeptide chain (Vilotte et al. 1991). According to the strong similarity between bovine α-la (Vilotte et al. 1987) and human lysozyme (similar molecular weight, the same number of S-S bonds, identical N and C terminal residues; Peters et al. 1989), it has been proposed that both genes arose from a common ancestor (Vilotte et al. 1991).

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