Yohimbine reversal of ketamine-xylazine immobilization of raccoons (Procyon lotor).

Six adult raccoons (Procyon lotor) were sedated with a combination of ketamine hydrochloride (KH) at 10 mg/kg body weight and xylazine hydrochloride (XH) at 2 mg/kg body weight intramuscularly (i.m.). Twenty min after the KH-XH combination was given, yohimbine hydrochloride (YH) at either 0.1 mg/kg (Trial 1) or 0.2 mg/kg (Trial 2) body weight or a saline control (Trial 3) was administered intravenously (i.v.). The time to arousal, time to sternal recumbency and time to walking were recorded. These times were significantly shortened after YH administration [e.g., mean time to walking (MTW) at 0.2 mg/kg YH = 23.7 min] as compared to the saline controls (MTW = 108.8 min). Heart and respiratory rates both increased after YH administration, while body temperature remained constant. A fourth trial was performed using a higher ratio of KH to XH (45:1 rather than 5:1) to mimic sedation as performed in the field. The mean time to arousal (MTA) and MTW in this trial (1.3 and 23.7 min, respectively) were significantly shorter than controls and similar to YH trials performed after immobilization with 5:1 KH-XH. Yohimbine hydrochloride may be useful in field studies that require sedation of raccoons using KH-XH combinations.

Identification of a chymotrypsin-like proteinase in human mast cells.

An antiserum was produced against a chymotryptic proteinase purified from human skin. The antiserum did not cross-react with human leukocyte cathepsin G and elastase, rat mast cell proteinase I, and human skin tryptase. Indirect immunofluorescent staining of frozen skin sections to localize the proteinase showed cytoplasmic staining of cells scattered about the papillary dermis and around blood vessels and appendages. Restaining these sections with toluidine blue revealed that the fluorescently stained cells contained metachromatically staining granules, the major distinguishing feature of mast cells. A similar correlation was found in lung tissue. Ultrastructural studies employing the ferritin bridge technique to immunologically identify the proteinase additionally localized the proteinase to mast cell granules. Biochemical and immunochemical characterization of chymotryptic activity solubilized from isolated human lung mast cells identified a chymotryptic proteinase that may be identical to the skin chymotryptic proteinase. These studies establish that human skin mast cells contain a chymotrypsin-like proteinase that is a granule constituent and provide evidence that indicates a comparable proteinase is also present in lung mast cells.