No abstract

The day surgery concept has been adopted and used widely. To date, there is limited in‐depth research that has reviewed patients' experiences convalescing from day surgery and the degree to which community, medical, allied health and social assistance is required. In addition, research indicates that day surgery patients' educational preparedness may influence patients' abilities to better self‐manage their postoperative recovery. Using a simple interrupted time series design, this study evaluated and compared the efficacy of the existing generic educational instructions with specially designed procedure‐specific instructions. During data collection within Stage 1 and Stage 2 all subjects were asked to complete the Postoperative Symptoms Diary that contained a specifically developed postoperative Symptom Measurement Scale and Symptom Management Index. These patients were interviewed, via telephone, on the 10th day after discharge. The findings revealed that 91% of patients stated they were satisfied having their operation as a day procedure while the most frequently reported symptoms were pain, tiredness and immobility. In addition, it was found that patients needed carer assistance for an average of 3 days. The enhanced teaching package had no effect on patient recovery and their ability to self‐manage. Thus, it was indicated that patient recovery and ability to self‐manage at home may be related to the patient's own healing abilities and understanding of self‐care.

Two capsid precursor subunits, which sediment on glycerol gradients at 13S and 14S, respectively, have been identified in cytoplasmic extracts of encephalomyocarditis virus-infected HeLa cells. The 13S subunit, which was detected after a 10-min pulse label with 3H-labeled amino acids, contained only capsid precursor chain A (mol wt 100,000). When the 10-min pulse label in such cells was chased for 20 min, the A-containing 13S subunit in the cytoplasmic extracts was replaced by a 14S subunit containing equimolar proportions of three chains: a, y, and a. This (e,y,a)-containing 14S subunit could be dissociated into 6S subunits with the same polypeptide composition. The sedimentation properties and the polypeptide stoichiometry of these three precursor subunits, when compared with those of the 13S, (8,'y,a)s, and 5S, (B,y,a), subunits derived by acid dissociation of purified virions, suggest the following structural assignments: 13S, (A) ; 14S, (e, y,a),; 6S, (w,y,a). The molecular weights of the individually isolated capsid chains were determined by gel filtration in 6 M guanidine hydrochloride to be: a, 36,000; a, 32,000; ,, 29,500; y, 26,500; and 6, 7,800. With the exception of the b-chain, these values are in reasonable agreement with the values previously determined by electrophoresis on sodium dodecyl sulfatepolyacrylamide gels. These data support the hypothesis that picornavirus capsids are assembled from identical protomers according to the following scheme: (A)-(A)5 _ (,y,a)s-(b,f,y,a)o n(evy,a)n where n is the number of immature protomers per virion. Picomaviruses contain four nonidentical polypeptide chains here designated a, ,S, y, and 6 (29). All four chains are generated by posttranslational cleavage of a single, large (mol wt 100,000) precursor, the A chain (3, 13, 17, 22). The virions also frequently contain traces of a fifth polypeptide, a, which is an uncleaved precursor of # and 6 chains (3, 13). The cardioviral (encephalomyocarditis [EMC ] virus, mouse Elberfeld [ME ] virus, mengovirus) chains A, a, a, ,B, y, and 6 correspond to the polioviral chains NCVP-la, VP-0, VP-1, VP-2, VP-3, and VP-4, respectively (13, 32). We have adopted the cardiovirus nomenclature which lends itself more readily to the description of oligomeric structures. Cytoplasmic extracts of poliovirus-infected HeLa cells contain two capsid-related structures, one sedimenting at 148 and the other at 73S (25-27). Both contain the capsid peptides

Picornaviruses in general are quite heat-labile in the absence &cations (Wallis & Melnick, ~96z). McGregor & Mayor (~968) showed that heating purified preparations of poliovirus and rhinovirus at 5o ° for 2 min. led to the extrusion of ribonucleoprotein strands. These results suggested that gentle heating of the virus particles at slightly lower temperatures might offer a more easily controllable method of degradation.Suspensions of purified rhino-and poliovirus (o.I ml.) were heated at 45 ° or 5 o° for various periods. After heating, the preparations were cooled immediately in an ice bath and specimens were prepared for electron microscopy. Poliovirus (LsC) when heated at 45 ° for 3o to 6o sec. appeared to lose portions of its capsid structure leaving 'holes' in the particle (Fig. 2). A diffuse amorphous core resembling a 'puffball' was then released from within the capsid leaving an empty shell (Fig. 2). This component was not demonstrated previously by McGregor & Mayor 0968). Upon further heating the core became progressively extended, and after Io min. at 5 °0 only long strands and empty capsids were observed.In contrast, rhinovirus preparations were much more stable morphologically at 45 ° than poliovirus preparations. When heated for I rain. at 45 ° the majority of rhinovirus particles appeared to be still intact. Even when heating at 45 ° was continued up to Io min., only about half of the particles had released their RNA. Many of these empty particles were degraded into smaller subunits and individual capsomeres (Fig. 3). At 50o the degradation of the rhinovirus particles progressed rapidly. After 1 rain. few intact particles were found and many of the empty particles were degraded. As heating was continued up to lo rain., strands similar to those found with the poliovirus became progressively extended. The empty particles formed after the release of the virus RNA seemed to be very unstable and were generally degraded into smaller subunits. In an effort to slow down this process the volume of the virus suspension was increased to 0"5 ml. This material was then incubated at 50 ° for ~ min. followed by rapid cooling. Under these conditions results were obtained similar to those observed with poliovirus. Amorphous cores appeared to be released from within the capsids, leaving empty capsids which appeared, in addition, to have portions of their structure missing (Fig. 4). The material released from within the capsids was associated with partially extended strands.Samples at various stages of degradation were treated with specific enzymes in order to determine the chemical composition of the components (Table ~). When the cores were treated with RNase before extension occurred they seemed to be completely digested. Once extension occurred, however, the strands were completely resistant to digestion with RNase unless they were first treated with pepsin. These observations suggested that the virus RNA was first released from within the particle. This was followed by its unfolding and association with a protei...

Cytoplasmic extracts of rhinovirus lA-infected HeLa cells, pulsed 15 min with [3H]leucine, contained a 13S subunit which was rich in the capsid precursor, peptide 92. After a 30-min chase, most of the capsid-related protein sedimented in a 14S peak that contained equimolar amounts ofthe capsid peptides e, a, and y, and some residual chain 92. The 14S subunit could be dissociated at pH 4.8 into 6S subunits containing only E, a, and y chains in equal proportions, indicating that the 14S subunit is an oligomer of (Eya) protomers. These subunits resemble subunits previously identified in the assembly of enteroviruses. These observations support the idea that rhinovirus assembly is basically similar to that of enteroviruses. Comparative studies on the peptide stoichiometry of the virion and the capsid precursor subunits indicate that rhinovirus 1A can contain as many as 11 immature protomers per virion. The picornaviruses have been divided (8) into EMC virus. This finding supports the view of a two genera: the acid-stable enteroviruses and common assembly pattern for both rhinovithe acid-labile rhinoviruses. Both enteroviruses and enteroviruses. ruses and rhinoviruses appear to be composed of 60 protomers, where each protomer is a pro-MATERIALS AND METHODS tein subunit composed of four nonidentical Media. Medium A is Eagle minimal medium in polypeptides (83y a). In the case ofthe cardiovi-Earle saline supplemented with 0.1 mM nonessenrus group (enteroviruses), the virion dissociates tial amino acids and 2 x 10-5 M inositol (7). Medium as if the protomers were held together by two B is a modification of medium A lacking calcium types of bonding domains (2, 4, 6). One domain chloride and containing 0.1% Pluronic F68 (7). Mebonds protomers together to form a pentameric dium AH is medium A containing 25 mM N-2-hysubunit; the second domain bonds 12 pentamers droxyethylpiperazine-N'-2-ethanesulfonic (HEPES) together to form the 60 subunit capsid. acid buffer, pH 7.4 (1). Medium AL is medium AH It has been suggested that the assembly of lacking amino acids. Medium P5 consists of Eagle minimal medium supplemented with 0.1% bovine the picornaviral capsid is also controlled by two serum albumin, 40 mM magnesium chloride, and 75 bonding sites (4, 11). Theoretically, assembly of ,ug of diethylaminoethyl dextran per ml (3). a 60-subunit shell, from such "bivalent" proto-Buffers. PBSA, buffer IV, and reticulocyte stanmers, can occur via one of three possible inter-dard buffer have been described (4). mediates: a dimer, a trimer, or a pentamer (11). Cells. Rhinovirus-sensitive HeLa cells, desig-Recent work on poliovirus (10) and encephalo-nated H-HeLa, were obtained from V. V. Hamparmyocarditis (EMC) virus (4) indicates that cap-ian,-Ohio State University (7). They were propasid assembly proceeds through a 14S subunit. gated in suspension in medium B supplemented sid as.mbly. oe through a 14S......subunit. with 10% bovine serum by shaking 300-ml cultures This subunit has been tentatively identified as in siliconized Florence flasks ...