Are site-specific airborne stimuli relevant for pigeon navigation only when matched by other release-site information?

1986 ◽  
Vol 73 (1) ◽  
pp. 42-43 ◽  
Author(s):  
J. Kiepenheuer
Keyword(s):  
Release Site ◽  
Site Specific ◽  
Pigeon Navigation

scholarly journals Tracking clock-shifted homing pigeons from familiar release sites

2000 ◽  
Vol 203 (2) ◽  
pp. 207-212 ◽  
Author(s):  
F. Bonadona ◽  
R. Holland ◽  
L. Dall'Antonia ◽  
T. Guilford ◽  
S. Benvenuti
Keyword(s):  
Large Scale ◽  
Release Site ◽  
Homing Pigeon ◽  
Homing Pigeons ◽  
Pigeon Navigation ◽  
Wrong Direction ◽  
Terrain Features ◽  
Clock Shift

Clock-shifted homing pigeons were tracked from familiar sites 17.1 km and 23.5 km from the home loft in Pisa, Italy, using an on-board route recorder. At the first release site, north of home, the majority of clock-shifted birds had relatively straight tracks comparable with those of control birds. At the second release site, south of home, the clock-shifted birds deflected in the direction predicted for the degree of clock shift, with many birds travelling some distance in the wrong direction before correcting their course. The possible role of large-scale terrain features in homing pigeon navigation is discussed.

Large-cluster and combined fluorescent and gold immunoprobes

1996 ◽  
Vol 54 ◽  
pp. 892-893
Author(s):  
Richard D. Powell ◽  
James F. Hainfeld ◽  
Carol M. R. Halsey ◽  
David L. Spector ◽  
Shelley Kaurin ◽  
...  
Keyword(s):  
Metal Cluster ◽  
Sulfonyl Chloride ◽  
Gel Filtration ◽  
Cross Linking ◽  
Site Specific ◽  
Fab Fragments ◽  
Cluster Label ◽  
Covalently Linked ◽  
Texas Red ◽  
Fold Excess

Two new types of covalently linked, site-specific immunoprobes have been prepared using metal cluster labels, and used to stain components of cells. Combined fluorescein and 1.4 nm “Nanogold” labels were prepared by using the fluorescein-conjugated tris (aryl) phosphine ligand and the amino-substituted ligand in the synthesis of the Nanogold cluster. This cluster label was activated by reaction with a 60-fold excess of (sulfo-Succinimidyl-4-N-maleiniido-cyclohexane-l-carboxylate (sulfo-SMCC) at pH 7.5, separated from excess cross-linking reagent by gel filtration, and mixed in ten-fold excess with Goat Fab’ fragments against mouse IgG (obtained by reduction of F(ab’)2 fragments with 50 mM mercaptoethylamine hydrochloride). Labeled Fab’ fragments were isolated by gel filtration HPLC (Superose-12, Pharmacia). A combined Nanogold and Texas Red label was also prepared, using a Nanogold cluster derivatized with both and its protected analog: the cluster was reacted with an eight-fold excess of Texas Red sulfonyl chloride at pH 9.0, separated from excess Texas Red by gel filtration, then deprotected with HC1 in methanol to yield the amino-substituted label.

The challenge of detecting modifications on proteins

2020 ◽  
Vol 64 (1) ◽  
pp. 135-153 ◽  
Author(s):  
Lauren Elizabeth Smith ◽  
Adelina Rogowska-Wrzesinska
Keyword(s):  
Mass Spectrometry ◽  
Protein Function ◽  
Chemical Properties ◽  
Lysine Acetylation ◽  
Mass Determination ◽  
Post Translational Modifications ◽  
Site Specific ◽  
The Common

Abstract Post-translational modifications (PTMs) are integral to the regulation of protein function, characterising their role in this process is vital to understanding how cells work in both healthy and diseased states. Mass spectrometry (MS) facilitates the mass determination and sequencing of peptides, and thereby also the detection of site-specific PTMs. However, numerous challenges in this field continue to persist. The diverse chemical properties, low abundance, labile nature and instability of many PTMs, in combination with the more practical issues of compatibility with MS and bioinformatics challenges, contribute to the arduous nature of their analysis. In this review, we present an overview of the established MS-based approaches for analysing PTMs and the common complications associated with their investigation, including examples of specific challenges focusing on phosphorylation, lysine acetylation and redox modifications.

MEMORY EFFECTS IN THE FRAGMENTATION OF MOLECULES FOLLOWING SITE-SPECIFIC CORE EXCITATION

1987 ◽  
Vol 48 (C9) ◽  
pp. C9-741-C9-744 ◽  
Author(s):  
W. HABENICHT ◽  
L. A. CHEWTER ◽  
M. SANDER ◽  
K. MÜLLER-DETHLEFS ◽  
E. W. SCHLAG
Keyword(s):  
Memory Effects ◽  
Core Excitation ◽  
Site Specific
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