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).

INTERFERENCE BY SERUM PROTEINS WITH LH RADIOIMMUNOASSAY USING IMMUNOSORBENT

1973 ◽  
Vol 72 (2) ◽  
pp. 235-242 ◽  
Author(s):  
A. M. Reuter ◽  
J. C. Hendrick ◽  
J. Sulon ◽  
P. Franchimont
Keyword(s):  
Molecular Weight ◽  
Human Serum ◽  
High Molecular Weight ◽  
Serum Proteins ◽  
Void Volume ◽  
High Molecular Weight Proteins ◽  
Serum Fractionation ◽  
Covalently Bound

ABSTRACT The percentage of LH* bound to antibodies that have been covalently bound to cellulose is diminished in the presence of LH-free human serum and sera from various species of animals. Serum fractionation studies on Sephadex G 200 show that the greatest interference comes from the proteins eluted in the void volume i. e. the high molecular weight proteins. Specifically, the gamma M globulins and the α2-macroglobulins appear to play an important role, as demonstrated by tests in which these proteins were neutralized by gamma M and α2-macroglobulin antisera.

Purification of Human Urokinase and its Topographical Localisation in Renal Parenchyma

1975 ◽  
Author(s):  
K. Andrassy ◽  
E. Ritz ◽  
U. Bleyl ◽  
R. Egbring
Keyword(s):  
Molecular Weight ◽  
Isoelectric Focusing ◽  
Gel Electrophoresis ◽  
Serum Proteins ◽  
Renal Tissue ◽  
Clot Lysis ◽  
Agar Gel ◽  
High Molecular Weight Complex ◽  
Zone Electrophoresis ◽  
Human Serum Proteins

Urokinase Leo was separated by agar zone electrophoresis into an anodic and cathodic fraction. The cathodic fraction, isolated from agar gel by ultracentrifugation, showed two precipitation bands with rabbit Urokinase antibodies. Band I displayed main Urokinase activity, in band II Urokinase was present in a high molecular weight complex with human serum proteins (albumin, a2-macroglobulin, a2HS glycoprotein); with affinity chromatography further separation of Urokinase isoenzymes from serum proteins was possible. The isoelectric point of these two Urokinase isoenzymes were pH 6.8 and pH 8.7 respectively in preliminary results with isoelectric focusing. Purification steps were controlled by disc gel electrophoresis and immunological techniques (Ouchterlony technique, Immunoelectrophoresis, clot lysis test with Urokinase antibodies).Topographic localisation of Urokinase in renal tissue, investigated with antibodies against Urokinase isoenzymes, revealed Urokinase activity both in the iuxtamedullary region (V. arcuatae, V. interlobulares, less V. recta) and in calyceal epithelia of the renal pelvis.

Suction effusion fluid from skin and constituent analysis: new candidate for interstitial fluid

1992 ◽  
Vol 263 (5) ◽  
pp. H1623-H1627 ◽  
Author(s):  
S. Kayashima ◽  
T. Arai ◽  
M. Kikuchi ◽  
N. Nagata ◽  
N. Ito ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Glucose Concentration ◽  
Interstitial Fluid ◽  
Serum Proteins ◽  
Blood Glucose Concentration ◽  
White Female ◽  
Absolute Pressure ◽  
Intravenous Glucose ◽  
Glucose Loading ◽  
Effusion Fluid

The authors analyzed the constituents of effuse transcutaneous fluid, labeled suction effusion fluid (SEF), and monitored its glucose concentration during glucose loading in rabbits (Japan White, female) under pentobarbital anesthesia. The SEF was sampled by suctioning corneal layer-stripped skin at 400 mmHg absolute pressure. The SEF proved to have nearly the same concentrations as serum for lower-molecular-weight substances such as glucose, creatinine, and urea nitrogens, but not for higher-molecular-weight substances such as serum proteins. The SEF protein concentration was one-fourth that of serum protein. Proteins > 100 kDa molecular mass were barely detectable in the SEF. Monitoring of SEF glucose change every 10 min during intravenous glucose loading was successfully accomplished, and SEF glucose concentration followed blood glucose concentration with a 10-min delay. The SEF was thought to consist of interstitial fluid and/or effuse fluid from small vessels in subcutaneous tissue.

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.

An AluI PCR-RFLP detecting a silent allele at the goat POU1F1 locus and its association with production traits

2007 ◽  
Vol 73 (1-3) ◽  
pp. 8-12 ◽  
Author(s):  
X.Y. Lan ◽  
C.Y. Pan ◽  
H. Chen ◽  
C.L. Zhang ◽  
J.Y. Li ◽  
...  
Keyword(s):  
Production Traits ◽  
Pcr Rflp ◽  
Silent Allele

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 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 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).

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