Characterization of fucosyltransferase activity during mouse spermatogenesis: evidence for a cell surface fucosyltransferase

Biochemistry ◽  
1989 ◽  
Vol 28 (4) ◽  
pp. 1611-1617 ◽  
Author(s):  
Richard A. Cardullo ◽  
D. Randall Armant ◽  
Clarke F. Millette
Keyword(s):  
Cell Surface ◽  
A Cell

Molecular Characterization of Trop-2, a Cell Surface Molecule Highly Expressed by Human Carcinomas — Cloning of the Gene Encoding Trop-2

1993 ◽  
pp. 75-82
Author(s):  
S. Alberti ◽  
M. Stella ◽  
R. Dell’ Arciprete ◽  
C. Bucci ◽  
A. Naglieri ◽  
...  
Keyword(s):  
Cell Surface ◽  
Molecular Characterization ◽  
Surface Molecule ◽  
Gene Encoding ◽  
Cell Surface Molecule ◽  
Human Carcinomas ◽  
A Cell

Biochemical Characterization of the Histidine Triad Protein PhtD as a Cell Surface Zinc-Binding Protein of Pneumococcus

Biochemistry ◽  
2011 ◽  
Vol 50 (17) ◽  
pp. 3551-3558 ◽  
Author(s):  
Elodie Loisel ◽  
Suneeta Chimalapati ◽  
Catherine Bougault ◽  
Anne Imberty ◽  
Benoit Gallet ◽  
...  
Keyword(s):  
Cell Surface ◽  
Biochemical Characterization ◽  
Binding Protein ◽  
Zinc Binding ◽  
A Cell

Isolation and partial characterization of a cell-surface heparan sulfate proteoglycan from embryonic rat spinal cord

1994 ◽  
Vol 37 (5) ◽  
pp. 584-595 ◽  
Author(s):  
J. M. Guiseppetti ◽  
J. B. McCarthy ◽  
P. C. Letourneau
Keyword(s):  
Spinal Cord ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Heparan Sulfate Proteoglycan ◽  
Partial Characterization ◽  
Sulfate Proteoglycan ◽  
Rat Spinal Cord ◽  
A Cell

scholarly journals Characterization of a Cell-surface Protein Antigen of Hydrophilic Streptococcus mutans Strain GS-5

Microbiology ◽  
1989 ◽  
Vol 135 (4) ◽  
pp. 981-988 ◽  
Author(s):  
H. Ohta ◽  
H. Kato ◽  
N. Okahashi ◽  
I. Takahashi ◽  
S. Hamada ◽  
...  
Keyword(s):  
Cell Surface ◽  
Streptococcus Mutans ◽  
Surface Protein ◽  
Protein Antigen ◽  
Cell Surface Protein ◽  
A Cell

scholarly journals Genetic Characterization of a Cell Envelope-Associated Proteinase from Lactobacillus helveticus CNRZ32

1999 ◽  
Vol 181 (15) ◽  
pp. 4592-4597 ◽  
Author(s):  
Jeffrey A. Pederson ◽  
Gerald J. Mileski ◽  
Bart C. Weimer ◽  
James L. Steele
Keyword(s):  
Cell Surface ◽  
Deletion Mutant ◽  
Cell Envelope ◽  
Physiological Role ◽  
Lactobacillus Helveticus ◽  
Whole Cells ◽  
A Cell ◽  
Hydrolysis Of

ABSTRACT A cell envelope-associated proteinase gene (prtH) was identified in Lactobacillus helveticus CNRZ32. TheprtH gene encodes a protein of 1,849 amino acids and with a predicted molecular mass of 204 kDa. The deduced amino acid sequence of the prtH product has significant identity (45%) to that of the lactococcal PrtP proteinases. Southern blot analysis indicates thatprtH is not broadly distributed within L. helveticus. A prtH deletion mutant of CNRZ32 was constructed to evaluate the physiological role of PrtH. PrtH is not required for rapid growth or fast acid production in milk by CNRZ32. Cell surface proteinase activity and specificity were determined by hydrolysis of αs1-casein fragment 1-23 by whole cells. A comparison of CNRZ32 and its prtH deletion mutant indicates that CNRZ32 has at least two cell surface proteinases that differ in substrate specificity.

Purification and characterization of a cell surface-associated esterase from Lactobacillus fermentum DT41

1997 ◽  
Vol 7 (1) ◽  
pp. 13-21 ◽  
Author(s):  
Marco Gobbetti ◽  
Emanuele Smacchi ◽  
Aldo Corsetti
Keyword(s):  
Cell Surface ◽  
Lactobacillus Fermentum ◽  
Purification And Characterization ◽  
A Cell

scholarly journals A Cell-Based Internalization and Degradation Assay with an Activatable Fluorescence–Quencher Probe as a Tool for Functional Antibody Screening

2015 ◽  
Vol 20 (7) ◽  
pp. 869-875 ◽  
Author(s):  
Yan Li ◽  
Peter Corbett Liu ◽  
Yang Shen ◽  
Marshall D. Snavely ◽  
Kaori Hiraga
Keyword(s):  
Cell Surface ◽  
Target Cells ◽  
Receptor Endocytosis ◽  
Drug Conjugates ◽  
Anti Cancer ◽  
A Cell ◽  
Rapid Characterization ◽  
Fluorescence Quencher ◽  
Culture Supernatants

For the development of therapeutically potent anti-cancer antibody drugs, it is often important to identify antibodies that internalize into cells efficiently, rather than just binding to antigens on the cell surface. Such antibodies can mediate receptor endocytosis, resulting in receptor downregulation on the cell surface and potentially inhibiting receptor function and tumor growth. Also, efficient antibody internalization is a prerequisite for the delivery of cytotoxic drugs into target cells and is critical for the development of antibody–drug conjugates. Here we describe a novel activatable fluorescence–quencher pair to quantify the extent of antibody internalization and degradation in the target cells. In this assay, candidate antibodies were labeled with a fluorescent dye and a quencher. Fluorescence is inhibited outside and on the surface of cells, but activated upon endocytosis and degradation of the antibody. This assay enabled the development of a process for rapid characterization of candidate antibodies potentially in a high-throughput format. By employing an activatable secondary antibody, primary antibodies in purified form or in culture supernatants can be screened for internalization and degradation. Because purification of candidate antibodies is not required, this method represents a direct functional screen to identify antibodies that internalize efficiently early in the discovery process.

Sign in / Sign up

Export Citation Format

Share Document