Orangeburg–Calhoun Technical College

This study investigates the effect of speed, tag and reader location, vehicle speed, and over-shadowing on RFID performance. The study tested two reader/antenna heights and three tag locations. Three vehicle speeds were tested for each tag location including the simultaneous placement of RFID tags on the vehicle. The study results show, with tags individually placed on the vehicle, the appropriate position for a tag is on the vehicle windshield, and the reader/antenna set at 7ft above the ground on a signpost. Placing multiple tags on the vehicle simultaneously improved the signal strength and detection rates. Vehicle speed had a negative effect on tag detection rate; that is, at higher vehicle speeds the detection rate decreased. With respect to horizontal distance between the reader and the tag, the results show that, the closer the tag and reader are to each other the higher the signal strength and so is the detection rate.

In Brief Refresh your knowledge of the role calcium plays in fluid and electrolyte balance, signs and symptoms of calcium imbalance, and how to interview quickly.

In Brief Refresh your knowledge of the role magnesium plays in fluid and electrolyte balance, signs and symptoms of magnesium imbalance, and how to interview quickly.

Back to table of contents Previous article Next article ArticleNo AccessCalcium and Extrapyramidal Side EffectsMOHAMED H. EL-DEFRAWIMOHAMED H. EL-DEFRAWISearch for more papers by this authorPublished Online:1 Apr 2006https://doi.org/10.1176/ajp.139.8.1079AboutSectionsPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack Citations ShareShare onFacebookTwitterLinked InEmail "Calcium and Extrapyramidal Side Effects." American Journal of Psychiatry, 139(8), p. 1079 Access content To read the fulltext, please use one of the options below to sign in or purchase access. Personal login Institutional Login Sign in via OpenAthens Purchase Save for later Item saved, go to cart PPV Articles - American Journal of Psychiatry $35.00 Add to cart PPV Articles - American Journal of Psychiatry Checkout Please login/register if you wish to pair your device and check access availability. Not a subscriber? Subscribe Now / Learn More PsychiatryOnline subscription options offer access to the DSM-5 library, books, journals, CME, and patient resources. This all-in-one virtual library provides psychiatrists and mental health professionals with key resources for diagnosis, treatment, research, and professional development. Need more help? PsychiatryOnline Customer Service may be reached by emailing [email protected] or by calling 800-368-5777 (in the U.S.) or 703-907-7322 (outside the U.S.). FiguresReferencesCited byDetailsCited byNone Volume 139Issue 8 August 1982Pages 1079-1079 Metrics PDF download History Published online 1 April 2006 Published in print 1 August 1982

Macrophages secrete a large number of proteases, implying in vivo exposure of the cell surface to proteolytic conditions. Mild trypsin treatment of 125I-labeled guinea pig peritoneal macrophages preferentially cleaves one surface component of apparent 160,000 mol wt. Similar trypsin treatment of macrophages with 3H-labeled carbohydrate surface moieties also cleaves a single 3H-labeled 160,000 mol wt glycoprotein, referred to as gp160. Nonreducing sodium dodecyl sulfate (SDS)-electrophoresis established that gp160 of trypsinized cells remains assembled in the membrane as a multichain disulfide- bonded molecule. gp160 was purified by detergent extraction, L. culinaris lectin affinity chromatography and DEAE-cellulose chromatography. The corresponding molecule from trypsinized cells was purified by the same procedure. Reducing SDS-electrophoresis of purified trypsinized 125I-labeled gp160 revealed two proteolytic fragments with apparent molecular weights of 85,000 and 71,000. Thus, mild trypsin treatment of macrophages preferentially cleaves a single surface protein, possibly at a single site. Because the two fragments of gp160 are accessible to lactoperoxidase and trypsin, both must be exposed on the membrane surface. The reactive carbohydrate site was found on the 85,000 mol wt fragment, which alone contains the 3H-label introduced into intact cells by neuraminidase, galactose, oxidase, and [3H]KBH4.