Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Method for analyzing a glycomolecule

a glycomolecule and structure technology, applied in the field of structure analysis of glycomolecules, can solve problems such as difficult analysis, and achieve the effect of facilitating access to glycomolecules and simplifying sample preparation and processing

Inactive Publication Date: 2005-08-25
PROCOGNIA ISRAEL
View PDF12 Cites 13 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Benefits of technology

[0007] Among the advantages of the method is simplified sample preparation and processing. The methods described herein eliminate the need for multiple pretreatment, treatment, purification, and buffer changing steps. In addition, the methods facilitate access to glycomolecules that are otherwise difficult to analyze. These glycans include, e.g., glycans in inter-subunit clefts or intra-subunit clefts of glycoproteins.

Problems solved by technology

In addition, the methods facilitate access to glycomolecules that are otherwise difficult to analyze.

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Method for analyzing a glycomolecule
  • Method for analyzing a glycomolecule
  • Method for analyzing a glycomolecule

Examples

Experimental program
Comparison scheme
Effect test

example 1

Comparative Glycomolecule Fingerprints of Desialized and Non-Desialized Glycoproteins

[0075] The glycomolecule fingerprint of human milk lactoferrin (hmLF) before and after disialyzation was examined. hmLF is a glycoprotein with a relatively simple glycosylation structure (Spik et al. Eur J Biochem. 1982;121(2):413-9). The hmLF structure includes two glycosylation sites that are occupied by any of 5 major glycans, resulting in 25 possible glycoforms. All of these glycans are of the complex bi-antennary type, containing a core fucose and differing in their levels of sialylation and the variable presence of antennary fucose (FIG. 1A). The various glycans differ in the presence of the (2,6) linked sialic acid residues and the (1,3) linked antennary fucose.

[0076] The fingerprints (FIG. 1B and FIG. 1C) were obtained by using a labeled anti-lactoferrin antibody as a probe. Twenty-four array-bound lectins were used and are grouped by their specificities on the abscissa. The group of compl...

example 2

Rule-Based Fingerprint Deconvolution

[0084] Deconvolution of the fingerprints is optimally performed by acquring a detailed understanding of lectin glycan recognition. This is complicated by the broadness of lectin specificities towards glycans, and by the fact that the affinities, both within and between the groups, differ markedly and are unknown. Measurement of these affinities are hampered by the inability to obtain a single-glycan-type glycoprotein for each glycan type. Mathematically, this translates into uncertainties in the conditional probabilities of observing a signal for a particular lectin, when the presence of a particular glycan is known. This limits the use of probabilistic-based algorithms.

[0085] An alternative approach using a rule-based expert system (Castillo et al., “Expert Systems and Probabilistic Network Models”—(Monographs in Computer Science) Springer-Verlag, New-York 1997) for fingerprint deconvolution was chosen. The rule base consists of lectin-glycan r...

example 3

Comparison of Glycomolecule Fingerprints Obtained Using Direct-Labeled Glycomolecules and Glycomolecule Fingerprints Obtained Using Labeled Lectins as Second Saccharide-Binding Agents

[0093] Fingerprint patterns obtained using direct labeling of the samples were compared to fingerprint patterns obtained using a labeled lectin to detect glycomolecules bound to a substrate.

[0094]FIGS. 2A-2C shows a fingerprints of a Bows melanoma cell-line derived tissue plasminogen activator (tPA). Fingerprints were obtained by direct labeling of the sample (FIG. 2A); labeling with a glucose / mannose recognizing lectin probe that recognizes both high-mannose and complex bi-antennary glycans (FIG. 2B); or with a glucose / mannose recognizing lectin probe that recognizes only high mannose type glycans (FIG. 2C). Since each of the fingerprints was obtained using a different probe, signals were corrected for the variation in fluorescence of the labeled probes (or sample, for the study shown in FIG. 2A), an...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

PropertyMeasurementUnit
Fluorescenceaaaaaaaaaa
Login to View More

Abstract

The invention relates generally the structural analysis of glycomolecule-containing macromolecules, such as those that occur either attached to proteins (proteoglycans, glycoproteins), lipids, or as free saccharides.

Description

RELATED APPLICATIONS [0001] This application claims the benefit of, and priority to, U.S. Ser. No. 60 / 531,578, filed Dec. 18, 2003. The contents of this application are incorporated herein by reference in their entirety.FIELD OF THE INVENTION [0002] The invention relates generally to the structural analysis of glycomolecules, which are molecules that contain carbohydrates and include carbohydrates attached to proteins (proteoglycans, glycoproteins), to lipids, or carbohydrates present as free polysaccharides. BACKGROUND OF THE INVENTION [0003] Mammalian glycoprotein oligosaccharides are commonly built from a limited number of monosaccharides. Nevertheless, structural diversity is vast, mainly due to complex branching patterns. Glycosylation sites on glycoproteins commonly display microheterogeneity in that they can be fully or partially occupied by structurally diverse oligosaccharides. Consequently, a glycoprotein is not typically isolated as a single structural entity, but rather ...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
IPC IPC(8): G01N33/53G01N33/537G01N33/543
CPCG01N33/5308G01N2400/02G01N2333/924G01N2333/42
Inventor AMOR, YEHUDITMARKMAN, OFERGULKO, MIRIT KOLOGSAMOKOVLISKY, ALBENAKLEINMAN, FREDIALERGAND, TALROSENFELD, RAKEFETMAYA, RUTHREBE, SABINAKASUTO, IDIL KELSONBANGIO, HAIM
Owner PROCOGNIA ISRAEL
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com