Free heavy chains

Renisio, J. G., Perez, J., Czisch, M., et al. (2002) Solution structure and backbone dynamics of an antigen-free heavy chain variable domain (VHH) from Llama. Proteins 47, 546-555. 

Siemankowski RF, Wiseman MO, White HD (1985) ADP dissociation from actomyosin subfragment 1 is sufficiently slow to limit the unloaded shortening velocity in vertebrate muscle. Proc Natl Acad Sci U S A 82 658662 Sivaramakrishnan M, Burke M (1982) The free heavy chain of vertebrate skeletal myosin subfragment 1 shows full enzymatic activity. J Biol Chem 257 11021105 Small JV (1977) Studies on isolated smooth muscle cells The contractOe apparatus. J Cell Sci 24 327349... 

Apart from a difference in specificity toward subtypes of MHC class I molecules, US2 and USl 1 seem to react dilfcrently with MHC class I heavy chains. In cells expressing US2 or USll newly synthesized MHC class I heavy chains are rapidly degraded, regardless of whether they are correctly folded and assembled in a complex with p2m or occur as free heavy chains (Wiertz et al. 1996a,b). In pulse-chase experiments, US2 coprecipitates with heavy chain-p2m complexes and with free heavy chains, whereas for USl 1 very little or no coprecipitation with class 1... 

Rajagopalan, S., and Brenner, M.B. Calnexin Retains Unassembled Major Histocompatibility Complex Class I Free Heavy Chains in the Endoplasmic Reticulum J. Exp. Med. 1994 180, 407-412. 

A disk or cone baffle located beneath the gas outlet duct may be beneficial if air in-leakage at the dust outlet cannot be avoided. A heavy chain suspended from the gas outlet duct has been found beneficial to minimize dust buildup on the cyclone walls in certain circumstances. Such a chain should be suspended from a swivel so that it is free to rotate without twisting. Substantially all devices that have been reported to reduce pressure drop do so by reducing spiral velocities in the cyclone chamber and consequently result in reduced collection efficiency. 

Bjork, I. and Tanford, C. 1971. Gross conformation of free polypeptide chains from rabbit immunoglobulin G. I. Heavy chain. Biochemistry 10, 1271-1280. 

The preferred Abs for ProteinChip experiments are Ag affinity purified polyclonal Abs (pAb), they exhibit a high avidity and slow off rate. In addition, Ab must be pure and intact ( 150 kDa), as contaminating proteins or free Ab light/heavy chains ( 25 and 50 kDa, respectively) will compete for active sites on the preactivated array and diminish the specific signal between the intact Ab and Ag (see Note 2). Further to this, it is important to assess the Ab buffer constituents the buffer must be free of amines (Tris, ethanolamine, azide) as this will also compete for the active sites and diminish the specific signal of the Ab/Ag interaction. 

Wold, L. E., Ceylan-Isik, A. F., Fang, C. X., Yang, X., Li, S. Y., Sreejayan, N., Privratsky, J. R., and Ren, J. 2006. Metallothionein alleviates cardiac dysfunction in streptozotocin-induced diabetes Role of Ca2+ cycling proteins, NADPH oxidase, poly(ADP-ribose) polymerase and myosin heavy chain isozyme. Free Radic. Biol. Med. 40 1419-1429. 

Bik release also occurs when Ial heavy chains are covalently transferred to hyaluronan in the extracellular matrix [23], This is a major component of cumulus cell-oocyte during fertilization and fibroblasts and mesothelial cells during inflammation. The heavy chains coupled to hyaluronan molecules bind to the cell surface through association with the hyaluronan receptor (CD44). The tumor necrosis factor-stimulated gene 6 (TSG-6) enhances the association of hyaluronan-linked heavy chains with CD44 and increases the release of free Bik [24, 25]. 

The labeling of BiP in mouse myeloma B cells by [ H]adenosine, suggestive of ADP-ribosylation, has been shown to be a modification found on BiP free of immunoglobulin heavy chains, but not on BiP bound to heavy chains (Hendershot et al., 1988). Additionally, the [ H]adenosine labeling parallels BiP phosphorylation in vivo conditions that increase BiP production decrease BiP phosphorylation and [ HJadenosine incorporation, suggesting that these two posttranslational modifications might modulate BiP activity in concert in some manner. 

Fig. 4. SDS-PAGE of FPLC purified MAbe. SDS mini-gel electrophoresis analysis of an FPLC-purified mouse MAb stained with Coomassie blue R. Track 1 shows standard mol-wt markers (for details see Fig. 2). The remaining tracks show different loadings of the same MAb. Characteristic heavy chains (60,000) and light chains (22,000) are clearly seen to be free of contamination by other proteins.

Protease-free preparation of CNTs can be obtained using an immobilized-metal-ion affinity chromatography (IMAC) step (Ros-setto et a/., 1992). This procedure is also useful for the purification of He, the 50 kDa carboxy-terminal part of the heavy chain of TeTx, which shows an identical retention time. However, IMAC-chromatography cannot be used for the purification of BoNT/D because this serotype is not retained. To obtain a protease-free BoNT/D preparation, an ion-exchange chromatography procedure was used (Schiavo and Montecucco, 1995). After freezing in liquid nitrogen, purified CNTs are stored at -80°C. 

In monoclonal gammopathies, the IFE patterns usually yield a distinct, sharply defined precipitin band with one heavy-chain and one light-chain antiserum. These bands match the location of the particular immunoglobulin in the reference pattern (Figure 20-10). A second, fainter band of free light chains may also be present. 

Termination of the autoxidation process occurs as peroxyl radicals couple to produce nonradical products. Additional sources of free radicals to initiate the free radical chain process include ultraviolet (UV) light and heavy metals (copper, iron, cobalt, manganese, and nickel) which catalyze oxidation by shortening the induction period and promoting free radical formation. 

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